Structure of Fmoc-Dab-OH
CAS No.: 161420-87-7
*Storage: {[sel_prStorage]}
*Shipping: {[sel_prShipping]}
The BI-3802 was designed by Boehringer Ingelheim and could be obtained free of charge through the Boehringer Ingelheim open innovation portal opnMe.com, associated with its negative control.
4.5
*For Research Use Only !
Change View
| Size | Price | VIP Price |
DE Stock US Stock |
Asia Stock Global Stock |
In Stock |
| {[ item.pr_size ]} |
Inquiry
{[ getRatePrice(item.pr_usd, 1,1,item.pr_is_large_size_no_price, item.pr_usd) ]} {[ getRatePrice(item.pr_usd,item.pr_rate,1,item.pr_is_large_size_no_price, item.discount_usd) ]} {[ getRatePrice(item.pr_usd, 1,1,item.pr_is_large_size_no_price, item.pr_usd) ]} |
Inquiry {[ getRatePrice(item.pr_usd,item.pr_rate,item.mem_rate,item.pr_is_large_size_no_price, item.vip_usd) ]} | {[ item.p_spot_brand_remark ]} 1-2 weeks {[ item.pr_usastock ]} In Stock Inquiry - | {[ item.p_spot_brand_remark ]} 1-2 weeks {[ item.pr_chinastock ]} {[ item.pr_remark ]} In Stock Inquiry - | Login - + |
Please Login or Create an Account to: See VIP prices and availability
Asia Stock: Ship in 3-5 business days
EU Stock: ship in 0-1 business day
Global Stock: ship in 5-7 days
US Stock: ship in 0-1 business day
Global Stock: ship in 5-7 days
{[ item.p_spot_brand_remark ]}
1-2weeks
Inquiry
Inquiry
{[ getRatePrice(item.pr_usd,item.pr_rate,item.mem_rate,item.pr_is_large_size_no_price, item.vip_usd) ]}
{[ getRatePrice(item.pr_usd, 1,1,item.pr_is_large_size_no_price, item.pr_usd) ]}
{[ getRatePrice(item.pr_usd,1,item.mem_rate,item.pr_is_large_size_no_price, item.pr_usd) ]}
{[ item.p_spot_brand_remark ]}
1-2weeks
Inquiry
Inquiry
{[ getRatePrice(item.pr_usd,item.pr_rate,1,item.pr_is_large_size_no_price, item.vip_usd) ]}
{[ getRatePrice(item.pr_usd, 1,1,item.pr_is_large_size_no_price, item.pr_usd) ]}
{[ getRatePrice(item.pr_usd, 1,1,item.pr_is_large_size_no_price, item.pr_usd) ]}
In Stock
- +
Please Login or Create an Account to: See VIP prices and availability
Asia Stock: Ship in 3-5 business days
EU Stock: ship in 0-1 business day
Global Stock: ship in 5-7 days
US Stock: ship in 0-1 business day
Global Stock: ship in 5-7 days
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
| CAS No. : | 161420-87-7 |
| Formula : | C19H20N2O4 |
| M.W : | 340.37 |
| SMILES Code : | O=C(O)[C@@H](NC(OCC1C2=C(C3=C1C=CC=C3)C=CC=C2)=O)CCN |
| MDL No. : | MFCD00237017 |
| InChI Key : | ZZDRDGKSMGGBDI-KRWDZBQOSA-N |
| Pubchem ID : | 7019708 |
| GHS Pictogram: |
|
| Signal Word: | Warning |
| Hazard Statements: | H315-H319-H335 |
| Precautionary Statements: | P261-P305+P351+P338 |
* 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 |
|---|---|---|
| 86.62% | With sodium hydroxide; In water; acetone; at 0 - 10℃; for 4h;pH 7.5 - 8; | B. The suspension 50g146 . 8nmol<strong>[161420-87-7]Fmoc-Dab-OH</strong> with 700 ml acetone: water = 1:in 1(v/v), in 0-10 °C add 38.4g176 . 1nmol (Boc)2O, 0.5NNaOH adjusting pH= 7.5-8, reaction 4 hours after Fmoc-Dab (Boc)-OH56g processing product, yield 86.62percent, HPLC99 . 4percent. The infrared, nuclear magnetic resonance confirmed correct structure, see Figure 3, Figure 4. |
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 86.5% | With [bis(acetoxy)iodo]benzene; In water; ethyl acetate; acetonitrile; at 20 - 30℃; for 72h; | A. The suspension 100g271 . 5nmolFmoc-Gln-OH with 2L ethyl acetate: acetonitrile: water = 2:1: mixed solution 1(v/v/v), in 20-30 C add 105.1g325 . 9nmolDipa, reaction 72 hours, post-processed to obtain product Fmoc-Dab-OH80g. Yield of 86.5%, HPLC: 99.6%. The infrared, nuclear magnetic resonance confirmed correct structure, see Figure 1, Figure 2. |
[ 29022-11-5 ]
[ 73724-45-5 ]
[ 116611-64-4 ]
[ 161420-87-7 ]

[ 1694-92-4 ]
[ 161420-87-7 ]
[ 911132-23-5 ]
[ 161420-87-7 ]
[ 911132-25-7 ]
[ 161420-87-7 ]
[ 193143-26-9 ]
[ 161420-87-7 ]
[ 71989-35-0 ]
[ 86123-10-6 ]
[ 161420-87-7 ]

[ 625845-42-3 ]
[ 71989-14-5 ]
[ 64-19-7 ]
[ 161420-87-7 ]
[ 378247-75-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: Synthesis of NH2-ACC-Rink Amide resin. Preparation of ACC wascarried out as described previously according to Maly et al.18 To glass reactionvessel, 1 eq (6.24 mmol, 13 g) of Rink AM resin was added and stirred gentlyonce per 10 min in DCM for 1 h, and then filtered and washed 3 times with DMF.Fmoc-protecting group was removed using 20% piperidine in DMF (5, 5, and25 min), filtered each time and washed with DMF (six times). Next, 2.50 eq of Fmoc-ACC-OH (15.6 mmol, 6.9 g) was preactivated with 2.50 eq HOBt monohydrate (15.6 mmol, 2.34 g) and 2.50 eq DICI (15.6 mmol, 2.0 ml) in DMFand mixture was added to the resin. Reaction was stirred gently for 24 h at room temperature. Resin was washed four times with DMF and reaction was repeatedusing 1.5 eq of above reagents to improve yield of ACC coupling to the resin. Afterreaction, resin was washed with DMF and Fmoc group was removed using 20%piperidine in DMF (5, 5, and 25 min), filtered and washed with DMF (six times). Synthesis of NH2-Asp(t-Bu)-ACC-Rink Amide resin. Next, 2.5 eqFmoc-Asp(t-Bu)-OH (15.6 mmol, 6.42 g) with 2.5 eq HATU (15.6 mmol, 5.93 g),2.5 eq collidine (15.6 mmol, 2.03 ml) in DMF were activated for 2 min and added tofilter cannula with 1 eq (6.24 mmol) NH2-ACC-resin and reaction was carried outfor 24 h. Next, resin was washed four times with DMF and reaction was repeatedusing 1.5 eq of above reagents. After washing with DMF, Fmoc-protecting groupwas removed using 20% piperidine in DMF (5, 5, and 25 min). Resin wasadditional washed with DCM (3 times) and MeOH (3 times) and dried over P2O5. Synthesis of individual optimized substrates. The 2.5 eqFmoc-P2-OH was preactivated with 2.5 eq HOBt and 2.5 eq DICI in DMF andadded to cartridge with 1 eq NH2-Asp(t-Bu)-ACC-resin (all substrates containedAsp at P1 position) and followed by gentle agitation for 3 h. Then, it was filteredand washed with DMF (six times). Fmoc-protecting group was removed using 20% piperidine in DMF (5, 5, and 25 min). Ninhydrin test was carried out each time aftercoupling and deprotection. A solution of 2.5 eq Fmoc-P3-OH, 2.5 eq HOBt, and2.5 eq DICI in DMF was added to the resin and the slurry was agitated for 3 h.After removal of the solution, the resin was washed with DMF (six times), andcoupling and deprotection of Fmoc-P4-OH was carried in identical conditions likeP2 position. N-terminus was protected with acetyl group using 5 eq AcOH, 5 eqHBTU, and 5 eq DIPEA in DMF as previous described. After solvent removal, theresin was washed with DMF (six times), DCM (three times), and MeOH (threetimes) dried over P2O5 and cleaved from the resin with a mixture of TFA/TIPS/H2O(%, v/v/v 95 : 2.5 : 2.5). The crude product was purified by HPLC and lyophilized.Its purity was confirmed by analytical HPLC. Each optimized substrate wasanalyzed using HRMS. Optimized substrates were dissolved in peptide gradeDMSO to 20mM concentration and stored at -80 Cuntil use. |

[ 29022-11-5 ]
[ 68858-20-8 ]
[ 118904-37-3 ]
[ 104091-09-0 ]
[ 71989-23-6 ]
[ 73724-45-5 ]
[ 73724-45-5 ]
[ 35737-15-6 ]
[ 161420-87-7 ]


[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35737-15-6 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 132684-60-7 ]
[ 135673-97-1 ]
[ 161420-87-7 ]
[ 158599-00-9 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: [0798] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mmol/g) was swollen in dry CH2C12 for 30 mm (7 ml CH2C12 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2C12/DMF (4/1) (10 ml per g resin) was added. Afier shaking for 2-4 h at it the resin was filtered off and washed successively with CH2C12, DMF, CH2C12, DMF and CH2C12. Then a solution of dry CH2C12/MeOH/DIPEA (17:2:1) was added (10 ml perg resin).Afier shaking for 3x30 mm the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2C12, DMF, CH2C12, MeOH, CH2C12, MeOH, CH2C12 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.[0803] After assembly of the linear peptide, the resin was suspended in 1 ml of 1% TFA in CH2C12 (v/v; 0.14 mmol) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml of 20% DIPEA in CH2C12 (v/v; 1.15 mmol). This procedure was repeated four times to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2C12. The CH2C12 layers containing product were evaporated to dryness.10804] The fully protected linear peptide was solubilised in8 ml of dry DMF. Then 2 eq. of HA11J and 2. eq. of HOAt in dry DMF (1-2 ml) and 4 eq. of DIPEA in dry DMF (1-2 ml) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 ml of CH2C12 and washed three times with 4.5 ml 10% acetonitrile in water (v/v). The CH2C12 layer was then evaporated to dryness.10805] To fully deprotect the peptide, 7 ml of cleavage cocktail TFADODT/thioanisol/H20 (87.5:2.5:5:5) were added, and the mixture was kept for 2.5-4 hat room tempera- tare until the reaction was completed. The reaction mixture was evaporated close to dryness and the peptide precipitated with 7 ml of cold Et20. The precipitate was washed 3 times with 4 ml of cold Et20. |
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35737-15-6 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 125238-99-5 ]
[ 132684-60-7 ]
[ 135673-97-1 ]
[ 161420-87-7 ]
[ 158599-00-9 ]

| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: [0798] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1percent crosslinked; loading: 1.4 mmol/g) was swollen in dry CH2C12 for 30 mm (7 ml CH2C12 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2C12/DMF (4/1) (10 ml per g resin) was added. Afier shaking for 2-4 h at it the resin was filtered off and washed successively with CH2C12, DMF, CH2C12, DMF and CH2C12. Then a solution of dry CH2C12/MeOH/DIPEA (17:2:1) was added (10 ml perg resin).Afier shaking for 3x30 mm the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2C12, DMF, CH2C12, MeOH, CH2C12, MeOH, CH2C12 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.[0803] After assembly of the linear peptide, the resin was suspended in 1 ml of 1percent TFA in CH2C12 (v/v; 0.14 mmol) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml of 20percent DIPEA in CH2C12 (v/v; 1.15 mmol). This procedure was repeated four times to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2C12. The CH2C12 layers containing product were evaporated to dryness.10804] The fully protected linear peptide was solubilised in8 ml of dry DMF. Then 2 eq. of HA11J and 2. eq. of HOAt in dry DMF (1-2 ml) and 4 eq. of DIPEA in dry DMF (1-2 ml) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 ml of CH2C12 and washed three times with 4.5 ml 10percent acetonitrile in water (v/v). The CH2C12 layer was then evaporated to dryness.10805] To fully deprotect the peptide, 7 ml of cleavage cocktail TFADODT/thioanisol/H20 (87.5:2.5:5:5) were added, and the mixture was kept for 2.5-4 hat room tempera- tare until the reaction was completed. The reaction mixture was evaporated close to dryness and the peptide precipitated with 7 ml of cold Et20. The precipitate was washed 3 times with 4 ml of cold Et20. |
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 71989-33-8 ]
[ 35737-15-6 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 135112-28-6 ]
[ 132684-60-7 ]
[ 161420-87-7 ]
[ 158599-00-9 ]


| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: [0798] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mmol/g) was swollen in dry CH2C12 for 30 mm (7 ml CH2C12 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2C12/DMF (4/1) (10 ml per g resin) was added. Afier shaking for 2-4 h at it the resin was filtered off and washed successively with CH2C12, DMF, CH2C12, DMF and CH2C12. Then a solution of dry CH2C12/MeOH/DIPEA (17:2:1) was added (10 ml perg resin).Afier shaking for 3x30 mm the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2C12, DMF, CH2C12, MeOH, CH2C12, MeOH, CH2C12 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.[0803] After assembly of the linear peptide, the resin was suspended in 1 ml of 1% TFA in CH2C12 (v/v; 0.14 mmol) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml of 20% DIPEA in CH2C12 (v/v; 1.15 mmol). This procedure was repeated four times to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2C12. The CH2C12 layers containing product were evaporated to dryness.10804] The fully protected linear peptide was solubilised in8 ml of dry DMF. Then 2 eq. of HA11J and 2. eq. of HOAt in dry DMF (1-2 ml) and 4 eq. of DIPEA in dry DMF (1-2 ml) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 ml of CH2C12 and washed three times with 4.5 ml 10% acetonitrile in water (v/v). The CH2C12 layer was then evaporated to dryness.10805] To fully deprotect the peptide, 7 ml of cleavage cocktail TFADODT/thioanisol/H20 (87.5:2.5:5:5) were added, and the mixture was kept for 2.5-4 hat room tempera- tare until the reaction was completed. The reaction mixture was evaporated close to dryness and the peptide precipitated with 7 ml of cold Et20. The precipitate was washed 3 times with 4 ml of cold Et20. |
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 71989-31-6 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 132684-60-7 ]
[ 161420-87-7 ]
[ 181954-34-7 ]
[ 143824-78-6 ]
[ 158599-00-9 ]

| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: [0798] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mmol/g) was swollen in dry CH2C12 for 30 mm (7 ml CH2C12 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2C12/DMF (4/1) (10 ml per g resin) was added. Afier shaking for 2-4 h at it the resin was filtered off and washed successively with CH2C12, DMF, CH2C12, DMF and CH2C12. Then a solution of dry CH2C12/MeOH/DIPEA (17:2:1) was added (10 ml perg resin).Afier shaking for 3x30 mm the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2C12, DMF, CH2C12, MeOH, CH2C12, MeOH, CH2C12 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.[0803] After assembly of the linear peptide, the resin was suspended in 1 ml of 1% TFA in CH2C12 (v/v; 0.14 mmol) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml of 20% DIPEA in CH2C12 (v/v; 1.15 mmol). This procedure was repeated four times to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2C12. The CH2C12 layers containing product were evaporated to dryness.10804] The fully protected linear peptide was solubilised in8 ml of dry DMF. Then 2 eq. of HA11J and 2. eq. of HOAt in dry DMF (1-2 ml) and 4 eq. of DIPEA in dry DMF (1-2 ml) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 ml of CH2C12 and washed three times with 4.5 ml 10% acetonitrile in water (v/v). The CH2C12 layer was then evaporated to dryness.10805] To fully deprotect the peptide, 7 ml of cleavage cocktail TFADODT/thioanisol/H20 (87.5:2.5:5:5) were added, and the mixture was kept for 2.5-4 hat room tempera- tare until the reaction was completed. The reaction mixture was evaporated close to dryness and the peptide precipitated with 7 ml of cold Et20. The precipitate was washed 3 times with 4 ml of cold Et20. |
[ 159610-93-2 ]
[ 35737-15-6 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 132684-60-7 ]
[ 135673-97-1 ]
[ 161420-87-7 ]

[ 158599-00-9 ]

| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: [0798] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1percent crosslinked; loading: 1.4 mmol/g) was swollen in dry CH2C12 for 30 mm (7 ml CH2C12 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2C12/DMF (4/1) (10 ml per g resin) was added. Afier shaking for 2-4 h at it the resin was filtered off and washed successively with CH2C12, DMF, CH2C12, DMF and CH2C12. Then a solution of dry CH2C12/MeOH/DIPEA (17:2:1) was added (10 ml perg resin).Afier shaking for 3x30 mm the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2C12, DMF, CH2C12, MeOH, CH2C12, MeOH, CH2C12 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.[0803] After assembly of the linear peptide, the resin was suspended in 1 ml of 1percent TFA in CH2C12 (v/v; 0.14 mmol) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml of 20percent DIPEA in CH2C12 (v/v; 1.15 mmol). This procedure was repeated four times to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2C12. The CH2C12 layers containing product were evaporated to dryness.10804] The fully protected linear peptide was solubilised in8 ml of dry DMF. Then 2 eq. of HA11J and 2. eq. of HOAt in dry DMF (1-2 ml) and 4 eq. of DIPEA in dry DMF (1-2 ml) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 ml of CH2C12 and washed three times with 4.5 ml 10percent acetonitrile in water (v/v). The CH2C12 layer was then evaporated to dryness.10805] To fully deprotect the peptide, 7 ml of cleavage cocktail TFADODT/thioanisol/H20 (87.5:2.5:5:5) were added, and the mixture was kept for 2.5-4 hat room tempera- tare until the reaction was completed. The reaction mixture was evaporated close to dryness and the peptide precipitated with 7 ml of cold Et20. The precipitate was washed 3 times with 4 ml of cold Et20. |
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35737-15-6 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 161420-87-7 ]
[ 158599-00-9 ]
[ 296774-32-8 ]

| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: [0798] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mmol/g) was swollen in dry CH2C12 for 30 mm (7 ml CH2C12 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2C12/DMF (4/1) (10 ml per g resin) was added. Afier shaking for 2-4 h at it the resin was filtered off and washed successively with CH2C12, DMF, CH2C12, DMF and CH2C12. Then a solution of dry CH2C12/MeOH/DIPEA (17:2:1) was added (10 ml perg resin).Afier shaking for 3x30 mm the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2C12, DMF, CH2C12, MeOH, CH2C12, MeOH, CH2C12 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.[0803] After assembly of the linear peptide, the resin was suspended in 1 ml of 1% TFA in CH2C12 (v/v; 0.14 mmol) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml of 20% DIPEA in CH2C12 (v/v; 1.15 mmol). This procedure was repeated four times to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2C12. The CH2C12 layers containing product were evaporated to dryness.10804] The fully protected linear peptide was solubilised in8 ml of dry DMF. Then 2 eq. of HA11J and 2. eq. of HOAt in dry DMF (1-2 ml) and 4 eq. of DIPEA in dry DMF (1-2 ml) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 ml of CH2C12 and washed three times with 4.5 ml 10% acetonitrile in water (v/v). The CH2C12 layer was then evaporated to dryness.10805] To fully deprotect the peptide, 7 ml of cleavage cocktail TFADODT/thioanisol/H20 (87.5:2.5:5:5) were added, and the mixture was kept for 2.5-4 hat room tempera- tare until the reaction was completed. The reaction mixture was evaporated close to dryness and the peptide precipitated with 7 ml of cold Et20. The precipitate was washed 3 times with 4 ml of cold Et20. |
[ 161420-87-7 ]
[ 5006-22-4 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 37% | With sodium hydroxide; In tetrahydrofuran; at 0 - 20℃; for 1h; | (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-(cyclobutanecarboxamido)butanoic acid Cyclobutanecarbonyl chloride (69.7 mg, 0.588 mmol) and NaOH (0.705 mL, 0.705 mmol) were dropped at the same time to a stirred solution of <strong>[161420-87-7](S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-aminobutanoic acid</strong> (200 mg, 0.588 mmol) in THF (1.5 mL) and of NaOH (1N, 0.7 mL) at 0 C. The reaction mixture was allowed to stir at rt for 1 h at which time LC-MS showed desired product peak. The reaction solution was acidified with 1N HCl and extracted with EtOAc (60 mL*1). The crude was purified via flash chromatography (ISCO, silica gel, 12 g column; flow rate 30 mL/min, 100% DCM to 20% MeOH/DCM). Fractions containing the desired product were combined and dried via centrifugal evaporation to provide the title compound (92.6 mg, 37%). Analysis LCMS Condition A: Retention time=0.94 min; ESI-MS(+) m/z 423.1 (M+H) 1H NMR (400 MHz, methanol-d4) delta 7.80 (d, J=7.5 Hz, 2H), 7.72-7.65 (m, 2H), 7.43-7.36 (m, 2H), 7.35-7.28 (m, 2H), 4.41-4.32 (m, 2H), 4.28-4.15 (m, 2H), 3.20 (d, J=7.0 Hz, 1H), 3.08 (s, 1H), 2.31-2.04 (m, 6H), 1.97 (d, J=9.9 Hz, 1H), 1.84 (d, J=7.3 Hz, 2H) |
[ 4524-93-0 ]
[ 161420-87-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 33% | With sodium hydroxide; In tetrahydrofuran; at 0 - 20℃; for 1h; | (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-(cyclopentanecarboxamido)butanoic acid Cyclopentanecarbonyl chloride (78 mg, 0.588 mmol) and NaOH (0.705 mL, 0.705 mmol) were dropped at the same time to a stirred solution of <strong>[161420-87-7](S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-aminobutanoic acid</strong> (200 mg, 0.588 mmol) in THF (1.5 mL) and of NaOH (1N, 0.7 mL) at 0 C. The reaction mixture was allowed to stir at rt for 1 h at which time LC-MS showed desired product peak. The reaction solution was acidified with 1N HCl and extracted with EtOAc (60 mL*1). The crude materials were purified via flash chromatography (ISCO, silica gel, 12 g column; flow rate 30 mL/min, 100% DCM to 20% MeOH/DCM). Fractions containing the desired product were combined and dried via centrifugal evaporation to provide the title compound (84.1 mg, 33%). Analysis LCMS Condition A: Retention time=0.98 min; ESI-MS(+) m/z 437.1 (M+H) 1H NMR (400 MHz, methanol-d4) delta 7.79 (d, J=7.5 Hz, 2H), 7.72-7.64 (m, 2H), 7.42-7.35 (m, 2H), 7.34-7.26 (m, 2H), 4.41-4.30 (m, 2H), 4.26-4.14 (m, 2H), 3.24-3.13 (m, 1H), 2.59 (t, J=7.8 Hz, 1H), 2.05 (s, 1H), 1.91-1.62 (m, 8H), 1.64-1.50 (m, 2H) |
[ 98-88-4 ]
[ 161420-87-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 57% | With sodium hydroxide; In tetrahydrofuran; at 0 - 20℃; for 1h; | (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-benzamidobutanoic acid Benzoyl chloride (83 mg, 0.588 mmol) and NaOH (0.705 mL, 0.705 mmol) were dropped at the same time to a stirred solution of <strong>[161420-87-7](S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-aminobutanoic acid</strong> (200 mg, 0.588 mmol) in THF (1.5 mL) and of NaOH (1N, 0.7 mL) at 0 C. The reaction mixture was allowed to stir at rt for 1 h at which time LC-MS showed desired product peak. The reaction solution was acidified with 1N HCl and extracted with EtOAc (60 mL*1). The crude was purified via flash chromatography (ISCO, silica gel, 12 g column; flow rate 30 mL/min, 100% DCM to 20% MeOH/DCM). Fractions containing the desired product were combined and dried via centrifugal evaporation to provide the title compound (160 mg, 57%). Analysis LCMS Condition A: Retention time=0.97 min; ESI-MS(+) m/z 445.1 (M+H) 1H NMR (400 MHz, methanol-d4) delta 7.82 (t, J=8.6 Hz, 4H), 7.74-7.67 (m, 2H), 7.56-7.50 (m, 1H), 7.49-7.42 (m, 2H), 7.42-7.36 (m, 2H), 7.35-7.26 (m, 2H), 4.39 (dd, J=7.0, 2.0 Hz, 2H), 4.32-4.21 (m, 2H), 3.62-3.52 (m, 1H), 3.45-3.35 (m, 1H), 2.20 (d, J=5.1 Hz, 1H), 1.99 (d, J=8.1 Hz, 1H) |
[ 161420-87-7 ]
[ 2719-27-9 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 70% | With sodium hydroxide; In tetrahydrofuran; at 0 - 20℃; for 1h; | (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-(cyclohexanecarboxamido)butanoic acid Cyclohexanecarbonyl chloride (86 mg, 0.588 mmol) and NaOH (0.705 mL, 0.705 mmol) were dropped at the same time to a stirred solution of <strong>[161420-87-7](S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-aminobutanoic acid</strong> (200 mg, 0.588 mmol) in THF (1.5 mL) and of NaOH (1N, 0.7 mL) at 0 C. The reaction mixture was allowed to stir at rt for 1 h at which time LC-MS showed desired product peak. The reaction solution was acidified with 1N HCl and extracted with EtOAc (60 mL*1). The crude materials were purified via flash chromatography (ISCO, silica gel, 12 g column; flow rate 30 mL/min, 100% DCM to 20% MeOH/DCM). Fractions containing the desired product were combined and dried via centrifugal evaporation to provide the title compound (201 mg, 70%). Analysis LCMS Condition A: Retention time=1.01 min; ESI-MS(+) m/z 451.2 (M+H) 1H NMR (400 MHz, methanol-d4): delta 7.79 (d, J=7.5 Hz, 2H), 7.73-7.65 (m, 2H), 7.43-7.35 (m, 2H), 7.34-7.26 (m, 2H), 4.42-4.30 (m, 2H), 4.27-4.15 (m, 2H), 3.18 (d, J=7.3 Hz, 1H), 2.15 (s, 1H), 2.10-2.01 (m, 1H), 1.89-1.72 (m, 5H), 1.68 (d, J=10.3 Hz, 1H), 1.49-1.17 (m, 6H) |
[ 527-69-5 ]
[ 161420-87-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 41% | With sodium hydroxide; In tetrahydrofuran; at 0 - 20℃; for 1h; | (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-(furan-2-carboxamido)butanoic acid Furan-2-carbonyl chloride (77 mg, 0.588 mmol) and NaOH (0.705 mL, 0.705 mmol) were dropped at the same time to a stirred solution of <strong>[161420-87-7](S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-aminobutanoic acid</strong> (200 mg, 0.588 mmol) in THF (1.5 mL) and of NaOH (1N, 0.7 mL) at 0 C. The reaction mixture was allowed to stir at rt for 1 h at which time LC-MS showed desired product peak. The reaction solution was acidified with 1N HCl and extracted with EtOAc (60 mL*1). The crude was purified via flash chromatography (ISCO, silica gel, 12 g column; flow rate 30 mL/min, 100% DCM to 20% MeOH/DCM). Fractions containing the desired product were combined and dried via centrifugal evaporation to provide the title compound (107 mg, 41%). Analysis LCMS Condition A: Retention time=0.92 min; ESI-MS(+) m/z 435.0 (M+H) 1H NMR (400 MHz, methanol-d4) delta 7.80 (d, J=7.7 Hz, 2H), 7.73-7.66 (m, 2H), 7.63 (s, 1H), 7.44-7.35 (m, 2H), 7.34-7.26 (m, 2H), 7.09 (d, J=3.3 Hz, 1H), 6.56 (dd, J=3.4, 1.7 Hz, 1H), 4.41-4.35 (m, 2H), 4.28-4.19 (m, 2H), 3.51 (dd, J=13.8, 7.4 Hz, 1H), 3.43-3.34 (m, 1H), 2.24-2.12 (m, 1H), 1.94 (d, J=7.3 Hz, 1H) |

[ 161420-87-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| 288 mg | With N-ethyl-N,N-diisopropylamine; In N,N-dimethyl-formamide; at 20℃; | To a solution of crude(S)- 1 -tert-butyl 5-(perfluorophenyl) 2-(1 8-(tert-butoxy)-8-oxooctadecanamido)pentanedioate (455 mg, .63 mmol) in DMF (6300 tl) wasadded Hunig?sBase (440 tl, 2.52 mmol), then (S)-2-((((9H-fluoren-9- yl)methoxy)carbonyl)amino)-4-aminobutanoic acid (214 mg, 0.630 mmol). The mixture was stirred at rt overnight. The mixture was diluted with citric acid and extracted 3 times into EtOAc. The combined organic extracts were washed with brine, dried over MgSO4, filtered, and concentrated in vacuo. The residue waspurified by PREP HPLC: (50 X 250mm HPLC Sunfire C18 l0jim 10 to 100% A:B over 30 mm, 5 mm at 100%B (A is 90:10:0.1 water:MeOH:TFA; B is 90:10:0.1 MeOH:water:TFA)). The material eluted during the 100% B isocratic section, so the gradient was not necessary. Fractions were neutralized with Hunig?s base and concentrated on the speedvac. The residue was taken up in EtOAc and washed twicewith water and once with brine. The organic layer was dried over MgSO4, filtered,and concentrated in vacuo to afford (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-((S)-5 -(tert-butoxy)-4-( 1 8-(tert-butoxy)- 18-oxooctadecanamido)-5-oxopentanamido)butanoic acid (288 mg, 0.328 mmol, 52.1 % yield). |

[ 86123-10-6 ]
[ 35737-15-6 ]
[ 161420-87-7 ]

| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: In a reaction vessel, Fmoc-protected Rink amide MBHA resinwas first swelled in DMF for fifteen min. A solution of 20% piperidinein DMF was added and mixture shaken mechanically for15 min resulting in the removal of Fmoc group. The required Fmocprotected amino acids and coupling reagent 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) were placed in amino acid vessels sequentially. DMF was added to theamino acid vessel, which was subsequently added (by positivepressure of N2) to the reaction vessel containing the resin, followedby addition of N,N-diisppropylethylamine (DIEA). After 3 h of mechanicalshaking at ambient temperature, the solvent was drainedand the resin washed with DMF (3 x 5 min) followed by methanol(2 x 5 mL). The cycles of deprotection and coupling were repeatedtill the desired peptide chain length was obtained. The resin-boundpeptide was transferred to a round bottom flask, and simultaneousremoval of resin and protective groups was achieved by using acocktail combination of TFA:triisopropylsilane (TIPS):H2O[95:2.5:2.5] for 3 h. The crude peptide was filtered and purified onpreparative HPLC system, and analyzed using solvent system ofCH3CN-H2O-0.1% CF3COOH in the gradient system: 30 min gradient,30-100% CH3CN-H2O-0.1% CF3COOH at 215 nm. |
[ 86123-10-6 ]
[ 109425-55-0 ]
[ 35737-15-6 ]
[ 161420-87-7 ]

| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| General procedure: In a reaction vessel, Fmoc-protected Rink amide MBHA resinwas first swelled in DMF for fifteen min. A solution of 20% piperidinein DMF was added and mixture shaken mechanically for15 min resulting in the removal of Fmoc group. The required Fmocprotected amino acids and coupling reagent 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) were placed in amino acid vessels sequentially. DMF was added to theamino acid vessel, which was subsequently added (by positivepressure of N2) to the reaction vessel containing the resin, followedby addition of N,N-diisppropylethylamine (DIEA). After 3 h of mechanicalshaking at ambient temperature, the solvent was drainedand the resin washed with DMF (3 x 5 min) followed by methanol(2 x 5 mL). The cycles of deprotection and coupling were repeatedtill the desired peptide chain length was obtained. The resin-boundpeptide was transferred to a round bottom flask, and simultaneousremoval of resin and protective groups was achieved by using acocktail combination of TFA:triisopropylsilane (TIPS):H2O[95:2.5:2.5] for 3 h. The crude peptide was filtered and purified onpreparative HPLC system, and analyzed using solvent system ofCH3CN-H2O-0.1% CF3COOH in the gradient system: 30 min gradient,30-100% CH3CN-H2O-0.1% CF3COOH at 215 nm. |
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 71989-31-6 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 91000-69-0 ]
[ 135248-89-4 ]
[ 71989-31-6 ]
[ 116611-64-4 ]
[ 161420-87-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| Coupling of the First Protected Amino Acid Residue to the Resin 0.5 g of 2-chlorotritylchloride resin (100-200 mesh, copoly(styrene-1% DVB) polymer matrix, Cat. No. 01-64-0114, Novabiochem, Merck Biosciences Ltd.) (Barlos et al. Tetrahedron Lett. 1989, 30, 3943-3946) (1.4 mMol/g, 0.7 mmol) was filled into a dried flask. The resin was suspended in CH2Cl2 (2.5 ml) and, allowed to swell at room temperature under constant stirring for 30 min. The resin was treated with 0.49 mMol (0.7 eq) of the first suitably protected amino acid residue and 488 mul (4 eq) of diisopropylethylamine (DIEA) in CH2Cl2 (2.5 ml), the mixture was shaken at 25 C. for 4 hours. The resin was shaken (CH2Cl2/MeOH/DIEA: 17/2/1), 30 ml for 30 min; then washed in the following order with CH2Cl2 (1×), DMF (1×), CH2Cl2 (1×), MeOH (1×), CH2Cl2 (1×), MeOH (1×), CH2Cl2 (2×), Et2O (2×) and dried under vacuum for 6 hours. Loading was typically 0.6-0.9 mMol/g. The following preloaded resin was prepared: Fmoc-Pro-2-chlorotritylresin. Synthesis of the Fully Protected Peptide Fragment The synthesis was carried out on a Syro-peptide synthesizer (MultiSynTech GmbH) using 24 to 96 reaction vessels. In each vessel were placed approximately 60 mg (weight of the resin before loading) of the above resin. The following reaction cycles were programmed and carried out: Steps 3 to 6 are repeated to add each amino-acid. Analytical Method: Analytical HPLC retention times (RT, in minutes) were determined using a Jupiter Proteo 90 A column, 150×2.0 mm, (cod. 00E-4396-B0-Phenomenex) with the following solvents A (H2O+0.1% TFA) and B (CH3CN+0.1% TFA) and the gradient: 0 min: 95% A, 5% B; 0.5 min: 95% A, 5% B; 20 min: 40% A, 60% B; 21 min: 0% A, 100% B; 23 min: 0% A, 100% B; 23.1 min: 95% A, 5% B; 31 min: 95% A, 5% B. Formation of Disulfide beta-Strand Linkage After formation of the disulfide beta-strand linkage, the resin was suspended in 1 ml (0.14 mMol) of 1% TFA in CH2Cl2 (v/v) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml (1.15 mMol) of 20% DIEA in CH2Cl2 (v/v). This procedure was repeated twice to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2Cl2. The CH2Cl2 layer was evaporated to dryness. The volatiles were removed and 8 ml dry DMF were added to the tube. Then 2 eq. of HATU in dry DMF (1 ml) and 4 eq. of DIPEA in dry DMF (1 ml) were added to the peptide, followed by stirring for 16 h. The volatiles were evaporated to dryness. The crude cyclised peptide was dissolved in 7 ml of CH2Cl2 and extracted with 10% acetonitrile in H2O (4.5 ml) three times. The CH2Cl2 layer was evaporated to dryness. To deprotect the peptide fully, 3 ml of cleavage cocktail TFA:TIS:H2O (95:2.5:2.5) were added, and the mixture was kept for 2.5 h. The volatiles were evaporated to dryness and the crude peptide was dissolved in 20% AcOH in water (7 ml) and extracted with isopropyl ether (4 ml) for three times. The aqueous layer was collected and evaporated to dryness, and the residue was purified by preparative reverse phase HPLC. After lyophilisation the products were obtained as white powders and analysed by the HPLC-ESI-MS analytical method described above. The analytical data comprising purity after preparative HPLC and ESI-MS are given. The peptide was synthesized starting with the amino acid L-Pro which was grafted to the resin. Starting resin was Fmoc-Pro-2-chlorotrityl resin, which was prepared as described above. The linear peptide was synthesized on solid support according to the procedure described above in the following sequence: Resin-Pro-DPro-Lys-Gln-Tyr-Cys-Tyr-Arg-Dab-DPro-Ala-Ser-Cys-Ala-His-Tyr. A disulfide beta-strand linkage was introduced as described above. The product was cleaved from the resin, cyclized, deprotected and purified as indicated by preparative reverse phase LC-MS. After lyophilisation the product was obtained as white powder and analysed by the HPLC-ESI-MS analytical method described above ([M+2H]2+: 933.1; RT: 10.47; UV-purity: 72%). |
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 71989-31-6 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 91000-69-0 ]
[ 135248-89-4 ]
[ 71989-31-6 ]
[ 116611-64-4 ]
[ 161420-87-7 ]
| Yield | Reaction Conditions | Operation in experiment |
|---|---|---|
| Coupling of the First Protected Amino Acid Residue to the Resin 0.5 g of 2-chlorotritylchloride resin (100-200 mesh, copoly(styrene-1% DVB) polymer matrix, Cat. No. 01-64-0114, Novabiochem, Merck Biosciences Ltd.) (Barlos et al. Tetrahedron Lett. 1989, 30, 3943-3946) (1.4 mMol/g, 0.7 mmol) was filled into a dried flask. The resin was suspended in CH2Cl2 (2.5 ml) and, allowed to swell at room temperature under constant stirring for 30 min. The resin was treated with 0.49 mMol (0.7 eq) of the first suitably protected amino acid residue and 488 mul (4 eq) of diisopropylethylamine (DIEA) in CH2Cl2 (2.5 ml), the mixture was shaken at 25 C. for 4 hours. The resin was shaken (CH2Cl2/MeOH/DIEA: 17/2/1), 30 ml for 30 min; then washed in the following order with CH2Cl2 (1×), DMF (1×), CH2Cl2 (1×), MeOH (1×), CH2Cl2 (1×), MeOH (1×), CH2Cl2 (2×), Et2O (2×) and dried under vacuum for 6 hours. Loading was typically 0.6-0.9 mMol/g. The following preloaded resin was prepared: Fmoc-Pro-2-chlorotritylresin. Synthesis of the Fully Protected Peptide Fragment The synthesis was carried out on a Syro-peptide synthesizer (MultiSynTech GmbH) using 24 to 96 reaction vessels. In each vessel were placed approximately 60 mg (weight of the resin before loading) of the above resin. The following reaction cycles were programmed and carried out: Steps 3 to 6 are repeated to add each amino-acid. Analytical Method: Analytical HPLC retention times (RT, in minutes) were determined using a Jupiter Proteo 90 A column, 150×2.0 mm, (cod. 00E-4396-B0-Phenomenex) with the following solvents A (H2O+0.1% TFA) and B (CH3CN+0.1% TFA) and the gradient: 0 min: 95% A, 5% B; 0.5 min: 95% A, 5% B; 20 min: 40% A, 60% B; 21 min: 0% A, 100% B; 23 min: 0% A, 100% B; 23.1 min: 95% A, 5% B; 31 min: 95% A, 5% B. Formation of Disulfide beta-Strand Linkage After formation of the disulfide beta-strand linkage, the resin was suspended in 1 ml (0.14 mMol) of 1% TFA in CH2Cl2 (v/v) for 3 minutes and filtered, and the filtrate was neutralized with 1 ml (1.15 mMol) of 20% DIEA in CH2Cl2 (v/v). This procedure was repeated twice to ensure completion of the cleavage. The resin was washed three times with 1 ml of CH2Cl2. The CH2Cl2 layer was evaporated to dryness. The volatiles were removed and 8 ml dry DMF were added to the tube. Then 2 eq. of HATU in dry DMF (1 ml) and 4 eq. of DIPEA in dry DMF (1 ml) were added to the peptide, followed by stirring for 16 h. The volatiles were evaporated to dryness. The crude cyclised peptide was dissolved in 7 ml of CH2Cl2 and extracted with 10% acetonitrile in H2O (4.5 ml) three times. The CH2Cl2 layer was evaporated to dryness. To deprotect the peptide fully, 3 ml of cleavage cocktail TFA:TIS:H2O (95:2.5:2.5) were added, and the mixture was kept for 2.5 h. The volatiles were evaporated to dryness and the crude peptide was dissolved in 20% AcOH in water (7 ml) and extracted with isopropyl ether (4 ml) for three times. The aqueous layer was collected and evaporated to dryness, and the residue was purified by preparative reverse phase HPLC. After lyophilisation the products were obtained as white powders and analysed by the HPLC-ESI-MS analytical method described above. The analytical data comprising purity after preparative HPLC and ESI-MS are given. The peptide was synthesized starting with the amino acid L-Pro which was grafted to the resin. Starting resin was Fmoc-Pro-2-chlorotrityl resin, which was prepared as described above. The linear peptide was synthesized on solid support according to the procedure described above in the following sequence: Resin-Pro-DPro-Lys-Gln-Tyr-Cys-Tyr-Arg-Dab-DPro-Ala-Ser-Cys-Tyr-His-Tyr. A disulfide beta-strand linkage was introduced as described above. The product was cleaved from the resin, cyclized, deprotected and purified as indicated by preparative reverse phase LC-MS. After lyophilisation the product was obtained as white powder and analysed by the HPLC-ESI-MS analytical method described above ([M+2H]2+: 978.6; RT: 10.95; UV-purity: 82%). |
[ 252049-08-4 ]
[ 35661-60-0 ]
[ 73731-37-0 ]
[ 161420-87-7 ]

[ 35661-39-3 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 71989-31-6 ]
[ 117872-75-0 ]
[ 161420-87-7 ]
[ 147290-11-7 ]
