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CAS No. : | 86123-10-6 | MDL No. : | MFCD00062955 |
Formula : | C24H21NO4 | Boiling Point : | - |
Linear Structure Formula : | - | InChI Key : | SJVFAHZPLIXNDH-JOCHJYFZSA-N |
M.W : | 387.43 | Pubchem ID : | 978332 |
Synonyms : |
Fmoc-D-Phe-OH
|
Chemical Name : | Fmoc-D-Phe-OH |
Num. heavy atoms : | 29 |
Num. arom. heavy atoms : | 18 |
Fraction Csp3 : | 0.17 |
Num. rotatable bonds : | 8 |
Num. H-bond acceptors : | 4.0 |
Num. H-bond donors : | 2.0 |
Molar Refractivity : | 109.66 |
TPSA : | 75.63 Ų |
GI absorption : | High |
BBB permeant : | No |
P-gp substrate : | Yes |
CYP1A2 inhibitor : | No |
CYP2C19 inhibitor : | No |
CYP2C9 inhibitor : | Yes |
CYP2D6 inhibitor : | Yes |
CYP3A4 inhibitor : | No |
Log Kp (skin permeation) : | -5.37 cm/s |
Log Po/w (iLOGP) : | 2.71 |
Log Po/w (XLOGP3) : | 4.64 |
Log Po/w (WLOGP) : | 4.22 |
Log Po/w (MLOGP) : | 3.42 |
Log Po/w (SILICOS-IT) : | 4.04 |
Consensus Log Po/w : | 3.81 |
Lipinski : | 0.0 |
Ghose : | None |
Veber : | 0.0 |
Egan : | 0.0 |
Muegge : | 0.0 |
Bioavailability Score : | 0.56 |
Log S (ESOL) : | -5.1 |
Solubility : | 0.0031 mg/ml ; 0.00000801 mol/l |
Class : | Moderately soluble |
Log S (Ali) : | -5.95 |
Solubility : | 0.00043 mg/ml ; 0.00000111 mol/l |
Class : | Moderately soluble |
Log S (SILICOS-IT) : | -7.38 |
Solubility : | 0.0000162 mg/ml ; 0.0000000419 mol/l |
Class : | Poorly soluble |
PAINS : | 0.0 alert |
Brenk : | 0.0 alert |
Leadlikeness : | 3.0 |
Synthetic accessibility : | 3.94 |
Signal Word: | Warning | Class: | N/A |
Precautionary Statements: | P261-P305+P351+P338 | UN#: | N/A |
Hazard Statements: | H315-H319-H335 | Packing Group: | N/A |
GHS Pictogram: |
* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
25% | General procedure: 2CTC resin (0.47g,loading = 0.53mmol/g ) was swelled in DCM/DMF for 20min before use. Then,Fmoc-Dab-OAll (1mmol, 4 eq), 8 eq. DIEA and 4ml DMF were added to react withresin for 12hr. The resin was capped with 200 mlmethanol to quench the remaining 2-chlorotrityl chloride. Generally, thesubsequent coupling was carried out using a solution of 4 eq. Fmoc-amino acid,3.8 eq. HCTU, and 8 eq. DIEA in DMF at 30 oC. Each coupling steprequired 1hr and the resin was washed by DMF and DCM before Fmoc-deprotection. The Fmoc group wasremoved by treatment with 20% piperidine in DMF twice (5 min, 10 min) followedby DMF and DCM wash. Dde group wasremoved by treatment with 3% NH2NH2/DMF for 20min threetimes. Allyl group wasremoved by treatment with PhSiH3 (10 eq.), Pd(PPh3)4(2 eq.) in 50% DCM/50% DMF for 3 hrs. After deprotection, the resin waswashed with DCM, 0.5% sodium diethyldithiocarbamate in DMF and DMF severaltimes. The finalcyclization step was carried out with 4 eq. PyAOP, 4eq. HOAt and 8eq.NMM for12hr. The cleavage reagentwas chose as TFA/water/TIPS (95/2.5/2.5). It was added into the dry resinprewashed with DCM and the cleavage was carried out for 1.5 hr. The TFAsolution was concentrated by blowing with N2. The crude peptideswere obtained by precipitating with cold diethyl ether, purified bysemi-preparative HPLC and lyophilized to achieve pure product. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: Peptides were synthesized on a 0.10 mmol scale using a H-Pro-2-Chlorotrityl resin (0.76 meq/g) with a manual microwave synthesizer (CEM Discover SPS). Syntheses consisted of two repeated steps: (i) removal of the Fmoc group with 20percent piperidine (lx at rt for 2 min, 1× using microwave irradiation for 4 min at 75° C. with 30W), and (ii) single coupling of the incoming (0196) Fmoc-protected amino acid (3 eq) with HBTU (3 eq) and DIPEA (5 eq) in DMF using microwave irradiation (75° C., 5 min, 30W). A lower temperature was utilized for His (50° C.) to avoid epimerization. The Arg coupling utilized more Arg (5 eq), HBTU (5 eq), and DIPEA (7 eq), and a longer irradiation time (10 min). After completion of the syntheses, peptides were cleaved with either a 99:1 DCM:TFA solution or 1:1:8 acetic acid:TFE:DCM solution. The cleavage solutions were then concentrated and side-chain protected peptides were precipitated using ice-cold ethyl ether. Peptides were cyclized in DCM with BOP (3 eq) and HOBt (3 eq) overnight, and the DCM was removed under vacuum. Without further purification, the cyclized peptides were side-chain deprotected using a 95:2.5:2.5 TFA:TIS:H2O solution for 2 hrs, the solution was then concentrated, and peptides precipitated using ice-cold ethyl ether. (0197) Crude peptides were purified by reverse-phase HPLC using a Shimadzu system with a photodiode array detector and a semi-preparative RP-HPLC C18 bonded silica column (Vydac 218TP1010, 1.0×2.5 cm). The peptides were at least 95percent pure as assessed by analytical RP-HPLC in two diverse solvent systems and had the correct molecular weight by MALDI-MS (University of Minnesota Mass Spectrometry Lab) (Table 1). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: Peptides were synthesized on a 0.10 mmol scale using a H-Pro-2-Chlorotrityl resin (0.76 meq/g) with a manual microwave synthesizer (CEM Discover SPS). Syntheses consisted of two repeated steps: (i) removal of the Fmoc group with 20percent piperidine (lx at rt for 2 min, 1× using microwave irradiation for 4 min at 75° C. with 30W), and (ii) single coupling of the incoming (0196) Fmoc-protected amino acid (3 eq) with HBTU (3 eq) and DIPEA (5 eq) in DMF using microwave irradiation (75° C., 5 min, 30W). A lower temperature was utilized for His (50° C.) to avoid epimerization. The Arg coupling utilized more Arg (5 eq), HBTU (5 eq), and DIPEA (7 eq), and a longer irradiation time (10 min). After completion of the syntheses, peptides were cleaved with either a 99:1 DCM:TFA solution or 1:1:8 acetic acid:TFE:DCM solution. The cleavage solutions were then concentrated and side-chain protected peptides were precipitated using ice-cold ethyl ether. Peptides were cyclized in DCM with BOP (3 eq) and HOBt (3 eq) overnight, and the DCM was removed under vacuum. Without further purification, the cyclized peptides were side-chain deprotected using a 95:2.5:2.5 TFA:TIS:H2O solution for 2 hrs, the solution was then concentrated, and peptides precipitated using ice-cold ethyl ether. (0197) Crude peptides were purified by reverse-phase HPLC using a Shimadzu system with a photodiode array detector and a semi-preparative RP-HPLC C18 bonded silica column (Vydac 218TP1010, 1.0×2.5 cm). The peptides were at least 95percent pure as assessed by analytical RP-HPLC in two diverse solvent systems and had the correct molecular weight by MALDI-MS (University of Minnesota Mass Spectrometry Lab) (Table 1). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: Peptides were synthesized on a 0.10 mmol scale using a H-Pro-2-Chlorotrityl resin (0.76 meq/g) with a manual microwave synthesizer (CEM Discover SPS). Syntheses consisted of two repeated steps: (i) removal of the Fmoc group with 20percent piperidine (lx at rt for 2 min, 1× using microwave irradiation for 4 min at 75° C. with 30W), and (ii) single coupling of the incoming (0196) Fmoc-protected amino acid (3 eq) with HBTU (3 eq) and DIPEA (5 eq) in DMF using microwave irradiation (75° C., 5 min, 30W). A lower temperature was utilized for His (50° C.) to avoid epimerization. The Arg coupling utilized more Arg (5 eq), HBTU (5 eq), and DIPEA (7 eq), and a longer irradiation time (10 min). After completion of the syntheses, peptides were cleaved with either a 99:1 DCM:TFA solution or 1:1:8 acetic acid:TFE:DCM solution. The cleavage solutions were then concentrated and side-chain protected peptides were precipitated using ice-cold ethyl ether. Peptides were cyclized in DCM with BOP (3 eq) and HOBt (3 eq) overnight, and the DCM was removed under vacuum. Without further purification, the cyclized peptides were side-chain deprotected using a 95:2.5:2.5 TFA:TIS:H2O solution for 2 hrs, the solution was then concentrated, and peptides precipitated using ice-cold ethyl ether. (0197) Crude peptides were purified by reverse-phase HPLC using a Shimadzu system with a photodiode array detector and a semi-preparative RP-HPLC C18 bonded silica column (Vydac 218TP1010, 1.0×2.5 cm). The peptides were at least 95percent pure as assessed by analytical RP-HPLC in two diverse solvent systems and had the correct molecular weight by MALDI-MS (University of Minnesota Mass Spectrometry Lab) (Table 1). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: The starting resin H-L-Leu-2CT (1006 mg, 0.674 mmol, 0.67 mmol/g) was pre-swollen in THF and then briefly washed with DCM (× 3) and DMF (×3). The appropriate Fmoc-amino acid (2 equiv.) was dissolved in a solution of HCTU (0.279 M, 1.8 equiv.), treated with 2,4,6-collidine (4 equiv.), and allowed to stand for 5 min. The pre-activated amino acid solution was added to the resin. After shaking for 2 hr, the solvent was drained and the resin was washed with DMF (× 3). Coupling efficiency was monitored by treatment of a small quantity of resin (1-3 mg) with 95:2.5:2.5 TFA/triisopropyl silane/H2O (10 muL) for 15 min, followed by suspension in 1:1 acetonitrile/H2O (1 mL), filtration and LC/MS analysis. In this manner, all couplings were deemed quantitative at each step. The Kaiser test was prone to false positives and was not a reliable indicator of coupling efficiency. If the next amino acid was not scheduled for immediate coupling, the resin was washed with DCM (× 3), IPA (× 3) and dried under vacuum overnight before storage; otherwise Fmoc deprotection was effected by two successive treatments of the resin with a solution of 30percent piperidine in DMF (ca. 10 mL per gram of resin) at ambient temperature (1 × 10 min, 1 × 20 min). The solvent was drained and the resin was washed with DMF (× 3) between each treatment, and after completion of the sequence. Peptide synthesis was completed by acylation of the N-terminus of AA-1 with 3-(R)-hydroxydecanoic acid (1.5 equiv.) using the same protocol outlined above. The resin was washed with DMF (× 3), DCM (× 3), IPA (× 3), DCM (× 3), IPA(× 3), and then dried under vacuum overnight. The final weight of the resin 1a was 2214 mg. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
2.5 mg | General procedure: The first four amino acids (from the C-terminus) of peptide 13 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used: The remaining two amino acids of peptide 13 were coupled manually using a 5-fold molar excess of amino acid, FIOBt and DIC (75 pmol each) in DMF as solvent. In addition, the whole sequence of peptide 15 was prepared by manual synthesis on a Rink amide AM resin using the same reagent conditions. Following coupling scheme was applied: In case of peptide 15, the resin was treated with a capping solution of 10 % DIPEA and 10 % acetic anhydride in DCM (15 min, 500 pi) after loading with the first C-terminal amino acid. Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). Peptides 14 and 16 were entirely prepared by automated peptide synthesis as described in the general section. The coupling scheme was as follows: The first two C-terminal amino acids of peptide 17 and 18 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used:The remaining three amino acids of peptide 17 and 18 were coupled manually using a 3-fold or 5- fold molar excess of the amino acid and a 5-fold molar excess of FIOBt and DIC (75 pmol each) in DMF as solvent. The coupling scheme was as follows: Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 pi each). For the removal of the Mmt protecting group in peptide 13, the resin was treated with a cleavage mixture consisting of 2 % TFA, 5 % TIS in DCM (8 x 2 min, 1 ml each). After each deprotection step, the resin was washed with DCM. Finally, the resin was incubated with 5 % DIPEA in DCM (2 x 10 min, 1 ml each). For the cleavage of the Dde protecting group in all other peptides (14-18), the resin was treated with 2 % hydrazine in DMF (10 x 10 min, 1 ml each). In case of peptide 14, the building block Fmoc-L-Dap(Mtt)-OFI was coupled manually in 3-fold molar excess with a 5-fold molar excess of FIOBt and DIC (75 pmol each) to the e-amino group of the C- terminal lysine. DMF was used as solvent and the coupling time was approximately 16 h. For peptide 16, the building block Fmoc-L-Dap(Fmoc)-OFI was coupled manually in 5-fold molar excess with FIOBt and DIC (75 pmol each) in DMF to the C-terminal lysine side-chain. The coupling time was 4 h. Subsequently, removal of the Fmoc protecting groups was achieved by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). 6-TAMRA was coupled manually to peptide 16 using a 2-fold molar excess of the fluorophore, FIATU and DIPEA (30 pmol each) in DMF as solvent for 5 h. Afterwards, removal of the Mtt protecting group in peptide 16 was performed as described for the Mmt deprotection above.The carbaboranes were coupled manually in 3-fold molar excess per free lysine or Dap amino group, except for mlJ9b, which was coupled in 1.5-fold molar excess per free amino group. Coupling reactions were prepared as follows: Peptides 13, 14 and 17: 3 eq. m9b, 5 eq. FIOBt and 5 eq. DIC in DMF as solvent. Peptide 15: 3 eq. bm9x, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 16: 3 eq. mlJ9b, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 18: 1.5 eq. mlJ9b, 2 eq. FIOBt and 2 eq. DIC in DMF. All coupling reactions were performed overnight for approximately 16 h. Cleavage of conjugates 13-15 and 17 from the resin and simultaneous side chain deprotection was accomplished using a mixture of TFA/TA/EDT (90:7:3, 1 ml) for 3 h. Cleavage of conjugates 16 and 18 from the resin was achieved using a mixture of TFA/FhO (95:5, 1 ml) for 3 h. The crude conjugates were precipitated and washed with an ice-cold mixture of hexane/diethyl ether (3:1, v/v), dissolved in ACN/FI2O and subsequently lyophilized. The first purification of the crude conjugate 13 was performed by preparative RP-HPLC using a C18- column (Phenomenex Jupiter 5u 300 A: 250 mm c 21.2 mm, 5 pm, 300 A) with a flow rate of 10 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. Conjugate 13 had to be purified a second time using a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. For purification of conjugate 14, a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 30 % to 60 % eluent B in A over 30 min was applied. Purification of the conjugates 15-17 was achieved using a Kinetex C18-column (Phenomenex Kinetex 5u XB-C18: 250 mm c 21.2 mm, 5 pm, 100 A) with a flow rate of 15 ml/min. For conjugate 15 and 16, a linear gradient of 40 % to 70 % eluent B in A over 30 min was used, whereas for conjugate 17 a gradient of 50 % to 80 % eluent B in A over 30 min was applied. Purification of the... |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
9.7 mg | General procedure: The first four amino acids (from the C-terminus) of peptide 13 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used: The remaining two amino acids of peptide 13 were coupled manually using a 5-fold molar excess of amino acid, FIOBt and DIC (75 pmol each) in DMF as solvent. In addition, the whole sequence of peptide 15 was prepared by manual synthesis on a Rink amide AM resin using the same reagent conditions. Following coupling scheme was applied: In case of peptide 15, the resin was treated with a capping solution of 10 % DIPEA and 10 % acetic anhydride in DCM (15 min, 500 pi) after loading with the first C-terminal amino acid. Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). Peptides 14 and 16 were entirely prepared by automated peptide synthesis as described in the general section. The coupling scheme was as follows: The first two C-terminal amino acids of peptide 17 and 18 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used:The remaining three amino acids of peptide 17 and 18 were coupled manually using a 3-fold or 5- fold molar excess of the amino acid and a 5-fold molar excess of FIOBt and DIC (75 pmol each) in DMF as solvent. The coupling scheme was as follows: Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 pi each). For the removal of the Mmt protecting group in peptide 13, the resin was treated with a cleavage mixture consisting of 2 % TFA, 5 % TIS in DCM (8 x 2 min, 1 ml each). After each deprotection step, the resin was washed with DCM. Finally, the resin was incubated with 5 % DIPEA in DCM (2 x 10 min, 1 ml each). For the cleavage of the Dde protecting group in all other peptides (14-18), the resin was treated with 2 % hydrazine in DMF (10 x 10 min, 1 ml each). In case of peptide 14, the building block Fmoc-L-Dap(Mtt)-OFI was coupled manually in 3-fold molar excess with a 5-fold molar excess of FIOBt and DIC (75 pmol each) to the e-amino group of the C- terminal lysine. DMF was used as solvent and the coupling time was approximately 16 h. For peptide 16, the building block Fmoc-L-Dap(Fmoc)-OFI was coupled manually in 5-fold molar excess with FIOBt and DIC (75 pmol each) in DMF to the C-terminal lysine side-chain. The coupling time was 4 h. Subsequently, removal of the Fmoc protecting groups was achieved by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). 6-TAMRA was coupled manually to peptide 16 using a 2-fold molar excess of the fluorophore, FIATU and DIPEA (30 pmol each) in DMF as solvent for 5 h. Afterwards, removal of the Mtt protecting group in peptide 16 was performed as described for the Mmt deprotection above.The carbaboranes were coupled manually in 3-fold molar excess per free lysine or Dap amino group, except for mlJ9b, which was coupled in 1.5-fold molar excess per free amino group. Coupling reactions were prepared as follows: Peptides 13, 14 and 17: 3 eq. m9b, 5 eq. FIOBt and 5 eq. DIC in DMF as solvent. Peptide 15: 3 eq. bm9x, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 16: 3 eq. mlJ9b, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 18: 1.5 eq. mlJ9b, 2 eq. FIOBt and 2 eq. DIC in DMF. All coupling reactions were performed overnight for approximately 16 h. Cleavage of conjugates 13-15 and 17 from the resin and simultaneous side chain deprotection was accomplished using a mixture of TFA/TA/EDT (90:7:3, 1 ml) for 3 h. Cleavage of conjugates 16 and 18 from the resin was achieved using a mixture of TFA/FhO (95:5, 1 ml) for 3 h. The crude conjugates were precipitated and washed with an ice-cold mixture of hexane/diethyl ether (3:1, v/v), dissolved in ACN/FI2O and subsequently lyophilized. The first purification of the crude conjugate 13 was performed by preparative RP-HPLC using a C18- column (Phenomenex Jupiter 5u 300 A: 250 mm c 21.2 mm, 5 pm, 300 A) with a flow rate of 10 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. Conjugate 13 had to be purified a second time using a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. For purification of conjugate 14, a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 30 % to 60 % eluent B in A over 30 min was applied. Purification of the conjugates 15-17 was achieved using a Kinetex C18-column (Phenomenex Kinetex 5u XB-C18: 250 mm c 21.2 mm, 5 pm, 100 A) with a flow rate of 15 ml/min. For conjugate 15 and 16, a linear gradient of 40 % to 70 % eluent B in A over 30 min was used, whereas for conjugate 17 a gradient of 50 % to 80 % eluent B in A over 30 min was applied. Purification of the... |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
2 mg | General procedure: The first four amino acids (from the C-terminus) of peptide 13 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used: The remaining two amino acids of peptide 13 were coupled manually using a 5-fold molar excess of amino acid, FIOBt and DIC (75 pmol each) in DMF as solvent. In addition, the whole sequence of peptide 15 was prepared by manual synthesis on a Rink amide AM resin using the same reagent conditions. Following coupling scheme was applied: In case of peptide 15, the resin was treated with a capping solution of 10 % DIPEA and 10 % acetic anhydride in DCM (15 min, 500 pi) after loading with the first C-terminal amino acid. Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). Peptides 14 and 16 were entirely prepared by automated peptide synthesis as described in the general section. The coupling scheme was as follows: The first two C-terminal amino acids of peptide 17 and 18 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used:The remaining three amino acids of peptide 17 and 18 were coupled manually using a 3-fold or 5- fold molar excess of the amino acid and a 5-fold molar excess of FIOBt and DIC (75 pmol each) in DMF as solvent. The coupling scheme was as follows: Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 pi each). For the removal of the Mmt protecting group in peptide 13, the resin was treated with a cleavage mixture consisting of 2 % TFA, 5 % TIS in DCM (8 x 2 min, 1 ml each). After each deprotection step, the resin was washed with DCM. Finally, the resin was incubated with 5 % DIPEA in DCM (2 x 10 min, 1 ml each). For the cleavage of the Dde protecting group in all other peptides (14-18), the resin was treated with 2 % hydrazine in DMF (10 x 10 min, 1 ml each). In case of peptide 14, the building block Fmoc-L-Dap(Mtt)-OFI was coupled manually in 3-fold molar excess with a 5-fold molar excess of FIOBt and DIC (75 pmol each) to the e-amino group of the C- terminal lysine. DMF was used as solvent and the coupling time was approximately 16 h. For peptide 16, the building block Fmoc-L-Dap(Fmoc)-OFI was coupled manually in 5-fold molar excess with FIOBt and DIC (75 pmol each) in DMF to the C-terminal lysine side-chain. The coupling time was 4 h. Subsequently, removal of the Fmoc protecting groups was achieved by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). 6-TAMRA was coupled manually to peptide 16 using a 2-fold molar excess of the fluorophore, FIATU and DIPEA (30 pmol each) in DMF as solvent for 5 h. Afterwards, removal of the Mtt protecting group in peptide 16 was performed as described for the Mmt deprotection above.The carbaboranes were coupled manually in 3-fold molar excess per free lysine or Dap amino group, except for mlJ9b, which was coupled in 1.5-fold molar excess per free amino group. Coupling reactions were prepared as follows: Peptides 13, 14 and 17: 3 eq. m9b, 5 eq. FIOBt and 5 eq. DIC in DMF as solvent. Peptide 15: 3 eq. bm9x, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 16: 3 eq. mlJ9b, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 18: 1.5 eq. mlJ9b, 2 eq. FIOBt and 2 eq. DIC in DMF. All coupling reactions were performed overnight for approximately 16 h. Cleavage of conjugates 13-15 and 17 from the resin and simultaneous side chain deprotection was accomplished using a mixture of TFA/TA/EDT (90:7:3, 1 ml) for 3 h. Cleavage of conjugates 16 and 18 from the resin was achieved using a mixture of TFA/FhO (95:5, 1 ml) for 3 h. The crude conjugates were precipitated and washed with an ice-cold mixture of hexane/diethyl ether (3:1, v/v), dissolved in ACN/FI2O and subsequently lyophilized. The first purification of the crude conjugate 13 was performed by preparative RP-HPLC using a C18- column (Phenomenex Jupiter 5u 300 A: 250 mm c 21.2 mm, 5 pm, 300 A) with a flow rate of 10 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. Conjugate 13 had to be purified a second time using a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. For purification of conjugate 14, a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 30 % to 60 % eluent B in A over 30 min was applied. Purification of the conjugates 15-17 was achieved using a Kinetex C18-column (Phenomenex Kinetex 5u XB-C18: 250 mm c 21.2 mm, 5 pm, 100 A) with a flow rate of 15 ml/min. For conjugate 15 and 16, a linear gradient of 40 % to 70 % eluent B in A over 30 min was used, whereas for conjugate 17 a gradient of 50 % to 80 % eluent B in A over 30 min was applied. Purification of the... |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
5.8 mg | General procedure: The first four amino acids (from the C-terminus) of peptide 13 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used: The remaining two amino acids of peptide 13 were coupled manually using a 5-fold molar excess of amino acid, FIOBt and DIC (75 pmol each) in DMF as solvent. In addition, the whole sequence of peptide 15 was prepared by manual synthesis on a Rink amide AM resin using the same reagent conditions. Following coupling scheme was applied: In case of peptide 15, the resin was treated with a capping solution of 10 % DIPEA and 10 % acetic anhydride in DCM (15 min, 500 pi) after loading with the first C-terminal amino acid. Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). Peptides 14 and 16 were entirely prepared by automated peptide synthesis as described in the general section. The coupling scheme was as follows: The first two C-terminal amino acids of peptide 17 and 18 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used:The remaining three amino acids of peptide 17 and 18 were coupled manually using a 3-fold or 5- fold molar excess of the amino acid and a 5-fold molar excess of FIOBt and DIC (75 pmol each) in DMF as solvent. The coupling scheme was as follows: Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 pi each). For the removal of the Mmt protecting group in peptide 13, the resin was treated with a cleavage mixture consisting of 2 % TFA, 5 % TIS in DCM (8 x 2 min, 1 ml each). After each deprotection step, the resin was washed with DCM. Finally, the resin was incubated with 5 % DIPEA in DCM (2 x 10 min, 1 ml each). For the cleavage of the Dde protecting group in all other peptides (14-18), the resin was treated with 2 % hydrazine in DMF (10 x 10 min, 1 ml each). In case of peptide 14, the building block Fmoc-L-Dap(Mtt)-OFI was coupled manually in 3-fold molar excess with a 5-fold molar excess of FIOBt and DIC (75 pmol each) to the e-amino group of the C- terminal lysine. DMF was used as solvent and the coupling time was approximately 16 h. For peptide 16, the building block Fmoc-L-Dap(Fmoc)-OFI was coupled manually in 5-fold molar excess with FIOBt and DIC (75 pmol each) in DMF to the C-terminal lysine side-chain. The coupling time was 4 h. Subsequently, removal of the Fmoc protecting groups was achieved by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). 6-TAMRA was coupled manually to peptide 16 using a 2-fold molar excess of the fluorophore, FIATU and DIPEA (30 pmol each) in DMF as solvent for 5 h. Afterwards, removal of the Mtt protecting group in peptide 16 was performed as described for the Mmt deprotection above.The carbaboranes were coupled manually in 3-fold molar excess per free lysine or Dap amino group, except for mlJ9b, which was coupled in 1.5-fold molar excess per free amino group. Coupling reactions were prepared as follows: Peptides 13, 14 and 17: 3 eq. m9b, 5 eq. FIOBt and 5 eq. DIC in DMF as solvent. Peptide 15: 3 eq. bm9x, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 16: 3 eq. mlJ9b, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 18: 1.5 eq. mlJ9b, 2 eq. FIOBt and 2 eq. DIC in DMF. All coupling reactions were performed overnight for approximately 16 h. Cleavage of conjugates 13-15 and 17 from the resin and simultaneous side chain deprotection was accomplished using a mixture of TFA/TA/EDT (90:7:3, 1 ml) for 3 h. Cleavage of conjugates 16 and 18 from the resin was achieved using a mixture of TFA/FhO (95:5, 1 ml) for 3 h. The crude conjugates were precipitated and washed with an ice-cold mixture of hexane/diethyl ether (3:1, v/v), dissolved in ACN/FI2O and subsequently lyophilized. The first purification of the crude conjugate 13 was performed by preparative RP-HPLC using a C18- column (Phenomenex Jupiter 5u 300 A: 250 mm c 21.2 mm, 5 pm, 300 A) with a flow rate of 10 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. Conjugate 13 had to be purified a second time using a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. For purification of conjugate 14, a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 30 % to 60 % eluent B in A over 30 min was applied. Purification of the conjugates 15-17 was achieved using a Kinetex C18-column (Phenomenex Kinetex 5u XB-C18: 250 mm c 21.2 mm, 5 pm, 100 A) with a flow rate of 15 ml/min. For conjugate 15 and 16, a linear gradient of 40 % to 70 % eluent B in A over 30 min was used, whereas for conjugate 17 a gradient of 50 % to 80 % eluent B in A over 30 min was applied. Purification of the... |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
5.5 mg | General procedure: The first four amino acids (from the C-terminus) of peptide 13 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used: The remaining two amino acids of peptide 13 were coupled manually using a 5-fold molar excess of amino acid, FIOBt and DIC (75 pmol each) in DMF as solvent. In addition, the whole sequence of peptide 15 was prepared by manual synthesis on a Rink amide AM resin using the same reagent conditions. Following coupling scheme was applied: In case of peptide 15, the resin was treated with a capping solution of 10 % DIPEA and 10 % acetic anhydride in DCM (15 min, 500 pi) after loading with the first C-terminal amino acid. Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). Peptides 14 and 16 were entirely prepared by automated peptide synthesis as described in the general section. The coupling scheme was as follows: The first two C-terminal amino acids of peptide 17 and 18 were coupled by automated peptide synthesis as described in the general section. Following coupling scheme was used:The remaining three amino acids of peptide 17 and 18 were coupled manually using a 3-fold or 5- fold molar excess of the amino acid and a 5-fold molar excess of FIOBt and DIC (75 pmol each) in DMF as solvent. The coupling scheme was as follows: Removal of Fmoc protecting groups after each manual coupling step was accomplished by using 20 % piperidine in DMF (2 x 10 min, 500 pi each). For the removal of the Mmt protecting group in peptide 13, the resin was treated with a cleavage mixture consisting of 2 % TFA, 5 % TIS in DCM (8 x 2 min, 1 ml each). After each deprotection step, the resin was washed with DCM. Finally, the resin was incubated with 5 % DIPEA in DCM (2 x 10 min, 1 ml each). For the cleavage of the Dde protecting group in all other peptides (14-18), the resin was treated with 2 % hydrazine in DMF (10 x 10 min, 1 ml each). In case of peptide 14, the building block Fmoc-L-Dap(Mtt)-OFI was coupled manually in 3-fold molar excess with a 5-fold molar excess of FIOBt and DIC (75 pmol each) to the e-amino group of the C- terminal lysine. DMF was used as solvent and the coupling time was approximately 16 h. For peptide 16, the building block Fmoc-L-Dap(Fmoc)-OFI was coupled manually in 5-fold molar excess with FIOBt and DIC (75 pmol each) in DMF to the C-terminal lysine side-chain. The coupling time was 4 h. Subsequently, removal of the Fmoc protecting groups was achieved by using 20 % piperidine in DMF (2 x 10 min, 500 mI each). 6-TAMRA was coupled manually to peptide 16 using a 2-fold molar excess of the fluorophore, FIATU and DIPEA (30 pmol each) in DMF as solvent for 5 h. Afterwards, removal of the Mtt protecting group in peptide 16 was performed as described for the Mmt deprotection above.The carbaboranes were coupled manually in 3-fold molar excess per free lysine or Dap amino group, except for mlJ9b, which was coupled in 1.5-fold molar excess per free amino group. Coupling reactions were prepared as follows: Peptides 13, 14 and 17: 3 eq. m9b, 5 eq. FIOBt and 5 eq. DIC in DMF as solvent. Peptide 15: 3 eq. bm9x, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 16: 3 eq. mlJ9b, 4 eq. FIOBt and 4 eq. DIC in DMF. Peptide 18: 1.5 eq. mlJ9b, 2 eq. FIOBt and 2 eq. DIC in DMF. All coupling reactions were performed overnight for approximately 16 h. Cleavage of conjugates 13-15 and 17 from the resin and simultaneous side chain deprotection was accomplished using a mixture of TFA/TA/EDT (90:7:3, 1 ml) for 3 h. Cleavage of conjugates 16 and 18 from the resin was achieved using a mixture of TFA/FhO (95:5, 1 ml) for 3 h. The crude conjugates were precipitated and washed with an ice-cold mixture of hexane/diethyl ether (3:1, v/v), dissolved in ACN/FI2O and subsequently lyophilized. The first purification of the crude conjugate 13 was performed by preparative RP-HPLC using a C18- column (Phenomenex Jupiter 5u 300 A: 250 mm c 21.2 mm, 5 pm, 300 A) with a flow rate of 10 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. Conjugate 13 had to be purified a second time using a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 50 % to 80 % eluent B in A over 30 min. For purification of conjugate 14, a XBridge C18-column (Waters XBridge Peptide BEH C18 OBD: 250 mm c 19 mm, 10 pm, 130 A) with a flow rate of 15 ml/min and a linear gradient of 30 % to 60 % eluent B in A over 30 min was applied. Purification of the conjugates 15-17 was achieved using a Kinetex C18-column (Phenomenex Kinetex 5u XB-C18: 250 mm c 21.2 mm, 5 pm, 100 A) with a flow rate of 15 ml/min. For conjugate 15 and 16, a linear gradient of 40 % to 70 % eluent B in A over 30 min was used, whereas for conjugate 17 a gradient of 50 % to 80 % eluent B in A over 30 min was applied. Purification of the... |
Tags: 86123-10-6 synthesis path| 86123-10-6 SDS| 86123-10-6 COA| 86123-10-6 purity| 86123-10-6 application| 86123-10-6 NMR| 86123-10-6 COA| 86123-10-6 structure
[ 352351-64-5 ]
(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(m-tolyl)propanoic acid
Similarity: 1.00
[ 352351-63-4 ]
(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(o-tolyl)propanoic acid
Similarity: 1.00
Precautionary Statements-General | |
Code | Phrase |
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Code | Phrase |
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P265 | Wash skin thouroughly after handling. |
P270 | Do not eat, drink or smoke when using this product. |
P271 | Use only outdoors or in a well-ventilated area. |
P272 | Contaminated work clothing should not be allowed out of the workplace. |
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P280 | Wear protective gloves/protective clothing/eye protection/face protection. |
P281 | Use personal protective equipment as required. |
P282 | Wear cold insulating gloves/face shield/eye protection. |
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Response | |
Code | Phrase |
P301 | IF SWALLOWED: |
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P305 | IF IN EYES: |
P306 | IF ON CLOTHING: |
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P321 | |
P322 | |
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P336 | Thaw frosted parts with lukewarm water. Do not rub affected area. |
P337 | If eye irritation persists: |
P338 | Remove contact lenses, if present and easy to do. Continue rinsing. |
P340 | Remove victim to fresh air and keep at rest in a position comfortable for breathing. |
P341 | If breathing is difficult, remove victim to fresh air and keep at rest in a position comfortable for breathing. |
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P350 | Gently wash with plenty of soap and water. |
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P352 | Wash with plenty of soap and water. |
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P362 | Take off contaminated clothing and wash before reuse. |
P363 | Wash contaminated clothing before reuse. |
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P371 | In case of major fire and large quantities: |
P372 | Explosion risk in case of fire. |
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P374 | Fight fire with normal precautions from a reasonable distance. |
P376 | Stop leak if safe to do so. Oxidising gases (section 2.4) 1 |
P377 | Leaking gas fire: Do not extinguish, unless leak can be stopped safely. |
P378 | |
P380 | Evacuate area. |
P381 | Eliminate all ignition sources if safe to do so. |
P390 | Absorb spillage to prevent material damage. |
P391 | Collect spillage. Hazardous to the aquatic environment |
P301 + P310 | IF SWALLOWED: Immediately call a POISON CENTER or doctor/physician. |
P301 + P312 | IF SWALLOWED: call a POISON CENTER or doctor/physician IF you feel unwell. |
P301 + P330 + P331 | IF SWALLOWED: Rinse mouth. Do NOT induce vomiting. |
P302 + P334 | IF ON SKIN: Immerse in cool water/wrap in wet bandages. |
P302 + P350 | IF ON SKIN: Gently wash with plenty of soap and water. |
P303 + P361 + P353 | IF ON SKIN (or hair): Remove/Take off Immediately all contaminated clothing. Rinse SKIN with water/shower. |
P304 + P312 | IF INHALED: Call a POISON CENTER or doctor/physician if you feel unwell. |
P304 + P340 | IF INHALED: Remove victim to fresh air and Keep at rest in a position comfortable for breathing. |
P304 + P341 | IF INHALED: If breathing is difficult, remove victim to fresh air and keep at rest in a position comfortable for breathing. |
P305 + P351 + P338 | IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continue rinsing. |
P306 + P360 | IF ON CLOTHING: Rinse Immediately contaminated CLOTHING and SKIN with plenty of water before removing clothes. |
P307 + P311 | IF exposed: call a POISON CENTER or doctor/physician. |
P308 + P313 | IF exposed or concerned: Get medical advice/attention. |
P309 + P311 | IF exposed or if you feel unwell: call a POISON CENTER or doctor/physician. |
P332 + P313 | IF SKIN irritation occurs: Get medical advice/attention. |
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P335 + P334 | Brush off loose particles from skin. Immerse in cool water/wrap in wet bandages. |
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P370 + P380 + P375 | In case of fire: Evacuate area. Fight fire remotely due to the risk of explosion. |
P371 + P380 + P375 | In case of major fire and large quantities: Evacuate area. Fight fire remotely due to the risk of explosion. |
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H242 | Heating may cause a fire |
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H260 | In contact with water releases flammable gases which may ignite spontaneously |
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H272 | May intensify fire; oxidizer |
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Health hazards | |
Code | Phrase |
H300 | Fatal if swallowed |
H301 | Toxic if swallowed |
H302 | Harmful if swallowed |
H303 | May be harmful if swallowed |
H304 | May be fatal if swallowed and enters airways |
H305 | May be harmful if swallowed and enters airways |
H310 | Fatal in contact with skin |
H311 | Toxic in contact with skin |
H312 | Harmful in contact with skin |
H313 | May be harmful in contact with skin |
H314 | Causes severe skin burns and eye damage |
H315 | Causes skin irritation |
H316 | Causes mild skin irritation |
H317 | May cause an allergic skin reaction |
H318 | Causes serious eye damage |
H319 | Causes serious eye irritation |
H320 | Causes eye irritation |
H330 | Fatal if inhaled |
H331 | Toxic if inhaled |
H332 | Harmful if inhaled |
H333 | May be harmful if inhaled |
H334 | May cause allergy or asthma symptoms or breathing difficulties if inhaled |
H335 | May cause respiratory irritation |
H336 | May cause drowsiness or dizziness |
H340 | May cause genetic defects |
H341 | Suspected of causing genetic defects |
H350 | May cause cancer |
H351 | Suspected of causing cancer |
H360 | May damage fertility or the unborn child |
H361 | Suspected of damaging fertility or the unborn child |
H361d | Suspected of damaging the unborn child |
H362 | May cause harm to breast-fed children |
H370 | Causes damage to organs |
H371 | May cause damage to organs |
H372 | Causes damage to organs through prolonged or repeated exposure |
H373 | May cause damage to organs through prolonged or repeated exposure |
Environmental hazards | |
Code | Phrase |
H400 | Very toxic to aquatic life |
H401 | Toxic to aquatic life |
H402 | Harmful to aquatic life |
H410 | Very toxic to aquatic life with long-lasting effects |
H411 | Toxic to aquatic life with long-lasting effects |
H412 | Harmful to aquatic life with long-lasting effects |
H413 | May cause long-lasting harmful effects to aquatic life |
H420 | Harms public health and the environment by destroying ozone in the upper atmosphere |
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