Name: 71989-38-3 | Fmoc-Tyr(tBu)-OH
Brand: Ambeed
SKU: A290914
Rating: 4.1 (44 reviews)

1
[ 86060-98-2 ]
[ 86060-87-9 ]
[ 71989-38-3 ]
[ 86061-01-0 ]
Fmoc-Arg(Mtr)-O-Pfp [ No CAS ]
[ 69558-55-0 ]

References: [1]Polish Journal of Chemistry,1992,vol. 66,p. 1269 - 1276.

2
[ 122889-11-6 ]
[ 35661-40-6 ]
[ 71989-38-3 ]
[ 35661-38-2 ]
Fmoc-Asp(OBzl)-OH [ No CAS ]
Tyr(tBu)-Asp(OBzl)-Phe-Phe-Ser(Bzl)-D-Ala [ No CAS ]

References: [1]Liebigs Annalen der Chemie,1993,p. 497 - 502.

3
[ 29022-11-5 ]
[ 35661-40-6 ]
[ 108-24-7 ]
[ 71989-38-3 ]
[ 198561-07-8 ]
Ac-Tyr-Asp-Phe-Gly-OH [ No CAS ]

References: [1]Organic Letters,2007,vol. 9,p. 2469 - 2472.

4
C₁₀H₁₅N₂O₅Pol [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 35661-38-2 ]
[ 71989-28-1 ]
[ 71989-16-7 ]
[ 71989-20-3 ]
[ 104091-08-9 ]
[ 143824-78-6 ]
C₄₂H₅₂N₇O₁₄Pol [ No CAS ]
C₄₄H₅₆N₇O₁₄Pol [ No CAS ]
C₄₅H₅₈N₇O₁₄Pol [ No CAS ]
C₄₅H₅₆N₇O₁₄Pol [ No CAS ]
C₄₆H₆₀N₇O₁₄Pol [ No CAS ]
C₄₅H₅₈N₇O₁₄PolS [ No CAS ]
C₄₆H₆₀N₇O₁₄Pol [ No CAS ]
C₄₈H₆₄N₇O₁₄Pol [ No CAS ]
C₄₇H₆₂N₇O₁₅Pol [ No CAS ]
C₄₇H₆₂N₇O₁₄PolS [ No CAS ]
C₄₇H₆₀N₇O₁₄Pol [ No CAS ]
C₄₈H₆₄N₇O₁₄Pol [ No CAS ]
C₄₉H₆₆N₇O₁₅Pol [ No CAS ]
C₄₈H₆₄N₇O₁₅Pol [ No CAS ]
C₄₉H₅₈N₇O₁₄Pol [ No CAS ]
C₅₁H₆₂N₇O₁₄Pol [ No CAS ]
C₅₀H₆₈N₇O₁₅Pol [ No CAS ]
C₄₅H₅₇N₈O₁₅Pol [ No CAS ]
C₄₇H₆₁N₈O₁₅Pol [ No CAS ]
C₄₉H₆₄N₇O₁₆Pol [ No CAS ]
C₅₃H₆₆N₇O₁₅Pol [ No CAS ]
C₅₁H₆₈N₇O₁₆Pol [ No CAS ]
C₅₁H₆₉N₈O₁₆Pol [ No CAS ]
C₅₃H₇₃N₈O₁₆Pol [ No CAS ]
C₅₆H₆₇N₈O₁₆Pol [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
	With O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate; N-ethyl-N,N-diisopropylamine; In DMF (N,N-dimethyl-formamide); at 20℃; for 12h;Combinatorial reaction / High throughput screening (HTS);	Split & Mix Procedure for the Resin Bound HexapeptideP-Glu (OAll)-Gly-X1X2X3X4-H sublibrary The resin was suspended in 3:1 mixture of 1,2-dichloroethane (DCE) and DMF and equally partitioned into 17 4 mL Alltech tubes. Each tube thus contained 0.1/17 mmol=5.88 10-6 mol of resin-bound dipeptide. Excess solvent was removed in vacuo, and the resin was suspended in DMF (200 mL) and agitated for 30 minutes. The 17 amino acids (1.76 10-5 mmol, 3 eq for each step, 7.04 10-5 mmol for 4 steps) were weighed into 17 vials: 1. Fmoc-Ala-OH 22 mg 2. Fmoc-Asn-OH 25 mg 3. Fmoc-Asp(OtBu)-OH 29 mg 4. Fmoc-Gln-OH 26 mg 5. <strong>[104091-08-9]Fmoc-Glu(OtBu)-OH</strong> 30 mg 6. Fmoc-Gly-OH 21 mg 7. Fmoc-Ile-OH 25 mg 8. Fmoc-Leu-OH 25 mg 9. Fmoc-Lys(BOC)-OH 33 mg 10. Fmoc-Met-OH 26 mg 11. Fmoc-Phe-OH 27 mg 12. Fmoc-Pro-OH 24 mg 13. Fmoc-Ser(tBu)-OH 27 mg 14. Fmoc-Thr(tBu)-OH 28 mg 15. Fmoc-Trp(BOC)-OH 37 mg 16. Fmoc-Tyr(tBu)-OH 32 mg 17. Fmoc-Val-OH 24 mg Each amino acid was dissolved in DMF (2 mL); an aliquot of each solution (0.5 mL, corresponding to 1.76 10-5 mmol, 3 eq of each amino acid) was added to the appropriate tube. TBTU (1.76 10-5 mmol×17=2.99 10-4, 96 mg) and DIPEA (1.76 10-5 mmol×17=2.99 10-4, 52 mL) were separately dissolved in DMF (1.7 mL) and each solution was evenly distributed, delivering 3 eq of each reagent, to each one of the 17 tubes.The reaction tubes were agitated at room temperature for 12 hours, then the reagents and solvents were removed in vacuo and the resin was rinsed with DMF (2×1 mL each tube), DCM (2×1 mL each tube) and methanol (2×1 mL each tube). The resin was then suspended in 3:1 mixture of 1,2-dichloroethane and DMF and recombined. The recombined resin was acetylated (3 mL of acetylating reagent, 1 hour, room temperature) and deprotected (3 mL of 20% piperidine in DMF, 2 hours, room temperature).The procedure was repeated 3 more times. At the end of the 4th amino acid coupling the deprotection step was not executed.

References: [1]Patent: US6909006,2005,B1 .Location in patent: Page/Page column 30-31; 37.

5
[ 68858-20-8 ]
[ 35661-40-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 96402-49-2 ]
[ 143824-78-6 ]
Fmoc-S-trityl penicillamine [ No CAS ]
C₆₁H₇₆N₁₀O₁₀S₂ [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2009,vol. 52,p. 3927 - 3940.

6
[ 68858-20-8 ]
[ 35661-40-6 ]
[ 71989-38-3 ]
[ 103213-32-7 ]
[ 109425-55-0 ]
[ 96402-49-2 ]
1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
Fmoc-S-trityl penicillamine [ No CAS ]
C₆₀H₇₄N₁₀O₁₀S₂ [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2009,vol. 52,p. 3927 - 3940.

7
(E)-17-[12-(N-fluorenylmethoxycarbonyl-L-valylamido)-4,7,10-trioxadodecanoyloxy]-4,7,10,13-tetraoxa-15-heptadecenoyl-β-alanyl-aminomethyl polystyrene [ No CAS ]
[ 5545-54-0 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-38-3 ]
[ 1172637-14-7 ]

References: [1]Synthesis,2009,p. 1355 - 1369.

8
Fmoc-Leu-Wang resin [ No CAS ]
[ 71989-31-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 132684-60-7 ]
[ 198561-07-8 ]
C₄₃H₆₉N₉O₉ [ No CAS ]

References: [1]Angewandte Chemie - International Edition,2010,vol. 49,p. 976 - 979.

9
knorr amide resin [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 96402-49-2 ]
[ 109425-56-1 ]
(2S,4R)-4-tert-butoxy-1-(9H-fluoren-9-ylmethoxycarbonyl)pyrrolidine-2-carboxylic acid [ No CAS ]
UGVCCGYKLC[NAL]OC-NH₂; O = L-trans-hydroxyproline; U = L-pyroglutamic acid; [NAL] = L-1-naphthylalanine [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2009,vol. 52,p. 6991 - 7002.

10
[ 158899-11-7 ]
[ 68858-20-8 ]
[ 71989-14-5 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 69558-55-0 ]

References: [1]Chemical Communications,2010,vol. 46,p. 2808 - 2810.

11
fmoc-Leu-Alko Resin [ No CAS ]
[ 159610-93-2 ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 71989-31-6 ]
[ 71989-38-3 ]
[ 64-19-7 ]
Ac-PLG-S(OMe)YL [ No CAS ]

References: [1]Bioorganic and Medicinal Chemistry Letters,2010,vol. 20,p. 853 - 856.

12
fmoc-Leu-Alko Resin [ No CAS ]
[ 110-15-6 ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-38-3 ]
Cap₁-PLG-S(OBn)YL; Cap₁ = succinic acid [ No CAS ]

References: [1]Bioorganic and Medicinal Chemistry Letters,2010,vol. 20,p. 853 - 856.

13
fmoc-Leu-Alko Resin [ No CAS ]
[ 123-43-3 ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-38-3 ]
[ 1218936-53-8 ]

References: [1]Bioorganic and Medicinal Chemistry Letters,2010,vol. 20,p. 853 - 856.

14
fmoc-Leu-Alko Resin [ No CAS ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 121-53-9 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-38-3 ]
Cap₃-PLG-S(OBn)YL; Cap₃ = 3-sulfobenzoic acid [ No CAS ]

References: [1]Bioorganic and Medicinal Chemistry Letters,2010,vol. 20,p. 853 - 856.

15
fmoc-Leu-Alko Resin [ No CAS ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-38-3 ]
[ 64-19-7 ]
Ac-PLG-S(OBn)YL [ No CAS ]

References: [1]Bioorganic and Medicinal Chemistry Letters,2010,vol. 20,p. 853 - 856.

16
Fmoc-Leu-Wang resin [ No CAS ]
[ 71989-31-6 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
[ 1198076-80-0 ]

References: [1]Angewandte Chemie - International Edition,2010,vol. 49,p. 976 - 979.

17
[ 68858-20-8 ]
[ 71989-14-5 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 143824-77-5 ]
[ 1207730-31-1 ]
[ 1207730-30-0 ]
[ 69558-55-0 ]

References: [1]Organic process research and development,2010,vol. 14,p. 1313 - 1325.

18
[ 68858-20-8 ]
[ 71989-14-5 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 143824-77-5 ]
[ 69558-55-0 ]
[ 75957-56-1 ]

References: [1]Organic process research and development,2010,vol. 14,p. 1313 - 1325.

19
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 71989-38-3 ]
[ 77128-73-5 ]
H-Tyr-Gly-Gly-(NMe)Phe-Leu-OH [ No CAS ]

References: [1]ACS Chemical Neuroscience,2013,vol. 4,p. 1204 - 1216.

20
[ 159610-89-6 ]
[ 68858-20-8 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 77284-32-3 ]
[ 94744-50-0 ]
N,N'-bis(tert-butyloxycarbonyl)-L-lysine dicyclohexylamine salt [ No CAS ]
[ 198561-07-8 ]
[ 1443329-49-4 ]

References: [1]Journal of Peptide Science,2013,vol. 19,p. 423 - 432.

21
aminomethylpolystyrene [ No CAS ]
[ 35661-40-6 ]
[ 108-24-7 ]
[ 71989-38-3 ]
[ 145069-56-3 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 221884-63-5 ]
C₈₂H₁₀₂N₁₁O₁₆PolS [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: For the synthesis of peptides affording a C-terminal acid (1, 2, 5, 6, 9, 10, 13, 14, 17, 18, 21, 22, 25, 26), AM-PS resin was initially swollen in CH2Cl2 (30 min) and subsequently reacted with Fmoc-AA-OCH2PhOCH2CH2CO2H (2.0equiv), and DIC (2.0equiv) in CH2Cl2 (2.0mL) for 2h at room temperature.27 The Kaiser test was negative.33 For the synthesis of peptides containing C-terminal amide (3, 4, 7, 8, 11, 12, 15, 16, 19, 20, 23, 24, 27, 28, 29), AM-PS resin was initially swollen in DMF (30 min) and subsequently reacted with Rink linker (5.0 equiv), DIC (5.0 equiv), and 6-Cl-HOBt (5.0equiv) in DMF (2.0 mL) for 2h at room temperature.27 The Kaiser test was negative.33 Fmoc SPPS was then performed on a Liberty 1 Microwave Peptide Synthesiser (CEM Corporation, Mathews, NC) on a 0.1 mmol scale using the Fmoc/tBu strategy. All amino acid couplings were performed as single coupling cycles, with the exception of Fmoc-Arg(Pbf) where a double coupling cycle was performed as part of a synthetic protocol recommended by CEM Microwave Technology. All Fmoc-AA couplings were performed using Fmoc-AA (5.0equiv, 0.2M), HBTU (4.5equiv, 0.45M), and iPrNEt (10equiv, 2M) in DMF, for 5 min, at 25W and maximum temperature of 75C, except Fmoc-Arg(Pbf) that was initially coupled for 25 min at room temperature which was followed by the second coupling for 3 min, at 25W and maximum temperature of 72C. Fmoc protecting group was removed using 5% piperazine in DMF (compounds 1-4) and 5% piperazine with 0.1M 6-Cl-HOBt in DMF (compounds 5-28). A 30s deprotection cycle was followed by a second deprotection for 3 min at 62W and maximum temperature of 75C. Acetylation was performed by treatment of the resin with acetic anhydride (20% in DMF) at room temperature (2×20min), or by using acetic anhydride (0.5M in NMP), iPr2EtN (0.125M in NMP) and acatalytic quantity of HOBt in NMP (room temperature, 2×5min). A fritted glass reaction vessel was used for the manual synthesis of 29 (0.25mmol scale). The Fmoc protecting group was deprotected with 20% piperidine solution in DMF (1×5min, 1×15min). The resin was washed with DMF (5×5mL), and Fmoc-AA coupling was performed. Nalpha-Fmoc-protected amino acid (4.0 equiv) was dissolved in DMF, HCTU (3.8 equiv) was added and mixture shaken until dissolved. The solution was transferred to the reaction vessel and shaken for 2min, followed by the addition of iPr2EtN (8.0 equiv). The mixture was shaken for 45min, filtered, and washed with DMF (3×5 mL). The resulting peptides were cleaved from the resin with simultaneous side chain protecting group removal by treatment with TFA/iPr3SiH/H2O/DODT (v/v/v/v; 94/1/2.5/2.5), for 2h at room temperature. The crude peptides were precipitated and triturated with cold diethyl ether, isolated (centrifugation), dissolved in 20% acetonitrile (aq) containing 0.1% TFA and lyophilized. Analytical reverse phase high-performance liquid chromatography (RP-HPLC) was performed using either a Dionex P680 or Dionex Ultimate U3000 system (flow rate of 1mL/min), using Waters XTerra column (MS C18, 150 mm×4.6 mm; 5mum) using gradient systems as indicated in the Supporting information. The solvent system used was A (0.1% TFA in H2O) and B (0.1% TFA in acetonitrile) with detection at 210nm, 254nm, and 280nm. The ratio of products was determined by integration of spectra recorded at 210nm. A Hewlett Packard (HP) 1100MSD mass spectrometer using ESI in the positive mode spectrometer was used for ESI-MS analysis (positive mode). Peptide purification was performed using a Waters 600E system using a semipreparative Phenomenex Gemini C18, 250mm×10mm; 5mum column or Phenomenex Luna C8, 250mm×10mm; 5mum column. Gradient systems were adjusted according to the elution profiles and peak profiles obtained from the analytical RP-HPLC chromatograms. Fractions were collected, analysed by either RP-HPLC or ESI-MS, pooled and lyophilised 3 times from 10mM aq HCl.

References: [1]Bioorganic and Medicinal Chemistry,2014,vol. 22,p. 3565 - 3572.

22
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 96402-49-2 ]
[ 109425-51-6 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
DCLGA-(L-1-naphthylalanyl)-RKCIPDNDKCCRPNLVCSRTHKWCKYVF-NH₂; disulfide linked (C2→C17, C9→C23, C16→C30) [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2015,vol. 58,p. 2299 - 2314.

23
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 71989-28-1 ]
[ 132388-59-1 ]
[ 96402-49-2 ]
[ 109425-51-6 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
DCLGF-(L-1-naphthylalanyl)-RKCIPDNDKCCRPNLVCSRTHKWCKYVF-NH₂; disulfide linked (C2→C17, C9→C23, C16→C30) [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2015,vol. 58,p. 2299 - 2314.

24
[ 29022-11-5 ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
[ 58-85-5 ]
[ 198561-07-8 ]
C₆₆H₉₄N₂₀O₂₁S [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: 4.1.1. Peptide synthesis; 4.1.2; Solid-phase peptide synthesis (SPPS) was performed with standardFmoc chemistry on rink amide resin using an automated peptidesynthesizer (Syro I, Multisyntech). The resin was loaded into a5 mL reactor with a frit at the bottom. Swelling was performed bydispensing 1 mL DMF and incubating for 15 min (2) with 10 sshaking every minute. Fmoc deprotection was achieved by treatmentwith 40percent piperidine DMF for 3 min and 20percent piperidine inDMF for 12 min (10 s/min shaking). Peptide couplings were carriedout by double couplings with Fmoc-protected amino acids(5 equiv), HBTU (5 equiv), HOBt (5 equiv) and DIPEA (10 equiv) inDMF for 40 min (10 s/min shaking). At the respective position,Fmoc-F2Pmp-OH (3 equiv) was coupled in DMF (1 mL) by manualaddition using TBTU (3 equiv), HOBt (3 equiv) and DIPEA (6 equiv)for 3 h, after 3 min preactivation. In case of the sequences for which side-chain labeling with biotinor carboxyfluorescein was planned, an additional 4-methyltrityl-(Mtt-) protected lysine was coupled to the N-terminus. Toselectively remove the Mtt group the resin was washed for 1 minwith DCM (3), deprotection was then achieved by treatment with1.8percent TFA in DCM for 3 min (10). During the deprotection the DCMsolution turned yellow.For fluorescein-labeling of the amine side-chain 5(6)-carboxyfluorescein(3 equiv), HATU (3 equiv), HOAt (3 equiv) andDIPEA (6 equiv) were dissolved in DMF and pre-activated for3 min. The solution was aspirated and coupling was allowed toproceed for 1 h. This step was repeated 4 times.For biotin-labeling of the amine side-chain the resin waswashed for 1 min in NMP (3). D-(+)-Biotin (3 equiv), HATU(3 equiv), HOAt (3 equiv) and DIPEA (6 equiv) were dissolved inNMP and pre-activated for 3 min. The solution was aspirated andcoupling was allowed to proceed for 2 h. This step was repeated2 times. N-terminal acetylation (where applicable) was achieved by dispensing800 lL of a mixture of acetic anhydride/pyridine (1:9) andreaction twice for 5 min (10 s/min shaking). After each deprotection,coupling or acetylation step, 5 washings (1 min each) withDMF were performed (10 s/min shaking).After synthesis the resin was transferred in a 5 mL syringeequipped with a frit, washed with DCM for 1 min (3) and driedin high vacuum for at least 30 min. For cleavage 1 mL of a mixtureof TFA and TIS (20:1) was added. The syringe with the mixture waskept on a shaker for 3 h. Then the liquid phase was filtered into20 mL of ice-cold Et2O. Formed precipitate was centrifuged,washed with ice-cold Et2O (2 20 mL) and purified by HPLC. 4.1.2. Azide functionalization of the N-terminus; To the peptides with the longer carbon linker, 6-azidohexanoicacid was coupled (with standard coupling conditions) to the Nterminalamine.The N-terminal amine of the peptides with the shorter linkerwas converted to an azide functionality directly on solid support.Using the compound imidazole-1-sulfonyl-azideHCl (synthesissee beneath) and modified conditions, which were reported forsolution phase chemistry from Goddard?Borger and Stick:8 Theresin was washed for 1 min each with DCM (2), DCM/MeOH(2) and MeOH (3). Then (for 40 mg resin, loading= 0.62 mmole/g) 1.4 equiv of imidazole-1-sulfonyl-azideHClin 1 mL MeOH and 100 ll of a saturated and centrifuged solutionof CuSO4*5H2O was added. After 1 min, DIPEA (1.8 equiv) wasadded and the coupling was allowed to proceed for 1 h andrepeated once more with an intermediate washing with MeOH(3 1 min).

References: [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 2848 - 2853.

25
[ 79598-53-1 ]
[ 29022-11-5 ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
[ 58-85-5 ]
[ 198561-07-8 ]
C₇₂H₁₀₅N₂₁O₂₂S [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: 4.1.1. Peptide synthesis; 4.1.2; Solid-phase peptide synthesis (SPPS) was performed with standardFmoc chemistry on rink amide resin using an automated peptidesynthesizer (Syro I, Multisyntech). The resin was loaded into a5 mL reactor with a frit at the bottom. Swelling was performed bydispensing 1 mL DMF and incubating for 15 min (2) with 10 sshaking every minute. Fmoc deprotection was achieved by treatmentwith 40percent piperidine DMF for 3 min and 20percent piperidine inDMF for 12 min (10 s/min shaking). Peptide couplings were carriedout by double couplings with Fmoc-protected amino acids(5 equiv), HBTU (5 equiv), HOBt (5 equiv) and DIPEA (10 equiv) inDMF for 40 min (10 s/min shaking). At the respective position,Fmoc-F2Pmp-OH (3 equiv) was coupled in DMF (1 mL) by manualaddition using TBTU (3 equiv), HOBt (3 equiv) and DIPEA (6 equiv)for 3 h, after 3 min preactivation. In case of the sequences for which side-chain labeling with biotinor carboxyfluorescein was planned, an additional 4-methyltrityl-(Mtt-) protected lysine was coupled to the N-terminus. Toselectively remove the Mtt group the resin was washed for 1 minwith DCM (3), deprotection was then achieved by treatment with1.8percent TFA in DCM for 3 min (10). During the deprotection the DCMsolution turned yellow.For fluorescein-labeling of the amine side-chain 5(6)-carboxyfluorescein(3 equiv), HATU (3 equiv), HOAt (3 equiv) andDIPEA (6 equiv) were dissolved in DMF and pre-activated for3 min. The solution was aspirated and coupling was allowed toproceed for 1 h. This step was repeated 4 times.For biotin-labeling of the amine side-chain the resin waswashed for 1 min in NMP (3). D-(+)-Biotin (3 equiv), HATU(3 equiv), HOAt (3 equiv) and DIPEA (6 equiv) were dissolved inNMP and pre-activated for 3 min. The solution was aspirated andcoupling was allowed to proceed for 2 h. This step was repeated2 times. N-terminal acetylation (where applicable) was achieved by dispensing800 lL of a mixture of acetic anhydride/pyridine (1:9) andreaction twice for 5 min (10 s/min shaking). After each deprotection,coupling or acetylation step, 5 washings (1 min each) withDMF were performed (10 s/min shaking).After synthesis the resin was transferred in a 5 mL syringeequipped with a frit, washed with DCM for 1 min (3) and driedin high vacuum for at least 30 min. For cleavage 1 mL of a mixtureof TFA and TIS (20:1) was added. The syringe with the mixture waskept on a shaker for 3 h. Then the liquid phase was filtered into20 mL of ice-cold Et2O. Formed precipitate was centrifuged,washed with ice-cold Et2O (2 20 mL) and purified by HPLC. 4.1.2. Azide functionalization of the N-terminus; To the peptides with the longer carbon linker, 6-azidohexanoicacid was coupled (with standard coupling conditions) to the Nterminalamine.The N-terminal amine of the peptides with the shorter linkerwas converted to an azide functionality directly on solid support.Using the compound imidazole-1-sulfonyl-azideHCl (synthesissee beneath) and modified conditions, which were reported forsolution phase chemistry from Goddard?Borger and Stick:8 Theresin was washed for 1 min each with DCM (2), DCM/MeOH(2) and MeOH (3). Then (for 40 mg resin, loading= 0.62 mmole/g) 1.4 equiv of imidazole-1-sulfonyl-azideHClin 1 mL MeOH and 100 ll of a saturated and centrifuged solutionof CuSO4*5H2O was added. After 1 min, DIPEA (1.8 equiv) wasadded and the coupling was allowed to proceed for 1 h andrepeated once more with an intermediate washing with MeOH(3 1 min).

References: [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 2848 - 2853.

26
[ 35661-60-0 ]
[ 35661-51-9 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 108-24-7 ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
Ac-Tyr-Asn-Trp-Asn-Ser-Phe-azaGly-Leu-Arg-Tyr-NH₂ [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2015,vol. 58,p. 3459 - 3470.

27
[ 67-56-1 ]
H-Gly-(2-Cl)-Trt-pol [ No CAS ]
[ 35661-39-3 ]
[ 291754-76-2 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-38-3 ]
[ 135673-97-1 ]
C₅₂H₇₅N₇O₁₄ [ No CAS ]

References: [1]Advanced Synthesis and Catalysis,2015,vol. 357,p. 2301 - 2309.

28
[ 35661-60-0 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 198561-07-8 ]
Ac-YLXKLLKLLXKLLK-NH₂; X=propargyl glicine [ No CAS ]

References: [1]Chemical Communications,2015,vol. 51,p. 14314 - 14317.

29
[ 214750-74-0 ]
[ 7021-11-6 ]
Fmoc-NH-γPhe(β-OH)-OH [ No CAS ]
C₃₁H₄₀N₄O₆ [ No CAS ]
[ 71989-38-3 ]
[ 356517-64-1 ]
[ 1301133-25-4 ]

References: [1]RSC Advances,2015,vol. 5,p. 94654 - 94657.

30
[ 16937-99-8 ]
3-acetamido-N-(2-aminoethyl)propanamide hydrogen chloride [ No CAS ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 1072-84-0 ]
Fmoc-D-Tyr(O-tBu)-OH [ No CAS ]
N²-(9-fluorenylmethyloxycarbonyl)-N³-(4-methyltrityl)-2,3-diaminopropanoic acid [ No CAS ]
Fmoc-D-4-Hpg(PG)-OH [ No CAS ]
C₅₀H₆₅N₁₃O₁₃ [ No CAS ]

References: [1]MedChemComm,2016,vol. 7,p. 132 - 140.

31
[ 16937-99-8 ]
3-acetamido-N-(2-aminoethyl)propanamide hydrogen chloride [ No CAS ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 1072-84-0 ]
Fmoc-D-Tyr(O-tBu)-OH [ No CAS ]
Nα-Fmoc-Nδ-(methyltrityl)-L-ornithine [ No CAS ]
Fmoc-D-4-Hpg(PG)-OH [ No CAS ]
C₅₂H₆₉N₁₃O₁₃ [ No CAS ]

References: [1]MedChemComm,2016,vol. 7,p. 132 - 140.

32
[ 16937-99-8 ]
3-acetamido-N-(2-aminoethyl)propanamide hydrogen chloride [ No CAS ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 1072-84-0 ]
Fmoc-D-Tyr(O-tBu)-OH [ No CAS ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
Fmoc-D-4-Hpg(PG)-OH [ No CAS ]
C₅₃H₇₁N₁₃O₁₃ [ No CAS ]

References: [1]MedChemComm,2016,vol. 7,p. 132 - 140.

33
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 71989-28-1 ]
[ 132388-59-1 ]
[ 96402-49-2 ]
[ 109425-51-6 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
XCLGFMRKCIPDNDKCCRPNLVCSRTHKWCKYVF amide; X=3-(1-naphthyl)-L-alanine [ No CAS ]