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Quality Control of Fmoc-Ala-OH Purity: 98% SDS Specification

COA

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NMR

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CNMR

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Product Details of Fmoc-Ala-OH

CAS No. :	35661-39-3
Formula :	C₁₈H₁₇NO₄
M.W :	311.33
SMILES Code :	C[C@H](NC(OCC1C2=C(C3=C1C=CC=C3)C=CC=C2)=O)C(O)=O
MDL No. :	MFCD00037139

Safety of Fmoc-Ala-OH

GHS Pictogram:
Signal Word:	Warning
Hazard Statements:	H302-H315-H319-H335
Precautionary Statements:	P261-P305+P351+P338

Application In Synthesis of Fmoc-Ala-OH

* 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.

Upstream synthesis route of [ 35661-39-3 ]
Downstream synthetic route of [ 35661-39-3 ]

[ 35661-39-3 ] Synthesis Path-Upstream 1~1

1
[ 35661-39-3 ]
[ 456-47-3 ]
[ 211617-68-4 ]
[ 133865-89-1 ]

References: [1] Journal of Medicinal Chemistry, 2007, vol. 50, # 20, p. 4909 - 4916.

[ 35661-39-3 ] Synthesis Path-Downstream 1~30

1
[ 29022-11-5 ]
[ 35661-39-3 ]
[ 35661-40-6 ]
[ 108-24-7 ]
[ 198561-07-8 ]
Ac-Ala-Asp-Phe-Gly-OH [ No CAS ]

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

2
C₃₄H₂₈N₂O₇ [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 103213-32-7 ]
[ 86060-81-3 ]
[ 116611-64-4 ]
[ 223416-45-3 ]

Yield	Reaction Conditions	Operation in experiment
		Chelmical synthesis: Peptides were synthesized on a Rink amide resin, 0.45 mmol/g [Fmoc-Cys(Trityl)-Wang; Novabiochem, San Diego, Calif.] usinig N-(9-fluorenyl)methoxycarboxyl chemistry and standard side chain protection except on cysteine residues. Cysteine residues were protected in pairs with either S-trityl on the first and third cysteines or S-acetamidomethyl on the second and fourth cysteines. Amino acid derivatives were from Advanced Chemtech (Louisville, Ky.). The peptides were removed from the resin and precipitated, and a two-step oxidation protocol was used to selectively fold the peptides as described previously (Luo et al., 1999). Briefly, the first disulfide bridge was closed by dripping the peptide into an equal volume of 20 mM potassium feliicyanide and 0.1 M Tris, pH 7.5. The solution was allowed to react for 30 min, and the monocyclic peptide was purified by reverse-phase HPLC. Simultaneous removal of the S-acetamidomethyl groups and closure of the second disulfide bridge was carried out by iodine oxidation. The monocyclic peptide and HPLC eluent was dripped into an equal volume of iodine (10 mM) in H20/trifluoroacetic acid/acetonitrile (78:2:20 by volume) and allowed to react for 10 min. The reaction was terminated by the addition of ascorbic acid diluted 20-fold with 0.1percent trifluoroacetic acid and the bicyclic product purified by HPLC. Mass Spectrometry: Measurements were performed at the Salk Institute for Biological Studies (San Diego, Calif.) under the direction of Jean Rivier. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry and liquid secondary ionization mass spectrometry were used.

References: [1]Patent: US2006/211623,2006,A1 .Location in patent: Page/Page column 9.

3
[ 29022-11-5 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 71989-26-9 ]
[ 198561-07-8 ]
NH₂-Pra-Lys(Boc)-Pra-Pro-Gly-Pra-Ala-Pra-Pro-Gly-OH [ No CAS ]

References: [1]Organic and Biomolecular Chemistry,2009,vol. 7,p. 4177 - 4185.

4
[ 29022-11-5 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 198561-07-8 ]
NH₂-Pra-Ala-Pra-Pro-Gly-Pra-Ala-Pra-Pro-Gly-OH [ No CAS ]

References: [1]Organic and Biomolecular Chemistry,2009,vol. 7,p. 4177 - 4185.

5
C₃₃H₃₄N₃O₅Pol [ No CAS ]
[ 29022-11-5 ]
[ 35661-39-3 ]
[ 122889-11-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-35-0 ]
[ 109425-51-6 ]
His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Ser(OBn)-[2-amino-3-(biphenyl-4-yl)propanoyl]-NH₂ [ No CAS ]

References: [1]Journal of Medicinal Chemistry,2009,vol. 52,p. 7788 - 7799.

6
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 71989-28-1 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
H-(propargylglycyl)-QGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIA-NH₂ [ No CAS ]

References: [1]Journal of Peptide Science,2011,vol. 17,p. 270 - 280.

7
[ 35661-39-3 ]
C₃₆H₃₇N₂O₆Pol [ No CAS ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 198561-07-8 ]
[ 684270-46-0 ]
C₂₆H₄₅N₉O₉ [ No CAS ]
[ 1372190-73-2 ]
[ 1372190-70-9 ]

Yield	Reaction Conditions	Operation in experiment
		Lys(Boc)-Pra-Asn(Trt)-Thr(tBu)-Ala-Thr(tBu)-Ala(N3)-Ala-Pal-PEG resin (16) (0.498 g, 0.09 mmol) was cleaved with TFA/iPr3SiH/H2O (v/v/v; 95/2.5/2.5, 5.0 mL) for 2 h, peptide was isolated as described in the general section to afford 47.3 mg of crude peptide 17. The crude peptide 17 (16.3 mg) was purified by RP-HPLC on a preparative Phenomenex Gemini C18, column at a flow rate of 5 mL min-1, using a linear gradient of 1percentB to 61percentB over 60 min (ca. 1percentB per minute) and lyophilised to give the title compound 17 as a white amorphous solid (4.9 mg, 18percent).

References: [1]Bioorganic and Medicinal Chemistry,2012,vol. 20,p. 2661 - 2668.

8
[ 35661-39-3 ]
C₃₆H₃₇N₂O₆Pol [ No CAS ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 198561-07-8 ]
[ 684270-46-0 ]
[ 1372190-73-2 ]
[ 1372190-65-2 ]

Yield	Reaction Conditions	Operation in experiment
		Lys(Boc)-Pra-Asn(Trt)-Thr(tBu)-Ala-Thr(tBu)-Ala(N3)-Ala-Pal-PEG resin (16) (0.498 g, 0.09 mmol) was cleaved with TFA/iPr3SiH/H2O (v/v/v; 95/2.5/2.5, 5.0 mL) for 2 h, peptide was isolated as described in the general section to afford 47.3 mg of crude peptide 17. The crude peptide 17 (16.3 mg) was purified by RP-HPLC on a preparative Phenomenex Gemini C18, column at a flow rate of 5 mL min-1, using a linear gradient of 1percentB to 61percentB over 60 min (ca. 1percentB per minute) and lyophilised to give the title compound 17 as a white amorphous solid (4.9 mg, 18percent). Purified Lys-Pra-Asn-Thr-Ala-Thr-Ala(N3)-Ala-NH2 (17) (4.4 mg, 5.42 x 10-3 mmol) was dissolved in a mixture of water and tert-butyl alcohol (1 : 2.5, 3.5 mL in total). A stock solution of CuSO4 (0.87 mg, 5.42 x 10-3 mmol) and sodium ascorbate (2.68 mg, 13.6 x 10-3 mmol) in water (1.5 mL) was added and the mixture was microwaved for 20 min at 80 °C in a sealed reaction vessel (120 W max) to afford crude peptide (8), containing inseparable dehydroalanine by-product. The crude peptide (8) was purified by RP-HPLC on a preparative Waters XTerra.(R). Prep. C18 column at a flow rate of 10 mL/min, using a linear gradient of 1percentB to 51percentB over 50 min (ca. 1percentB per minute). Fractions were lyophilised to give the title compound 8 as a white amorphous solid (0.7 mg, 18percent), containing inseparable dehydroalanine by-product.

References: [1]Bioorganic and Medicinal Chemistry,2012,vol. 20,p. 2661 - 2668.

9
[ 35661-39-3 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 198561-07-8 ]
[ 684270-46-0 ]
[ 1372190-74-3 ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: Fmoc SPPS was performed on a Liberty Microwave Peptide Synthesiser (CEM Corporation, Mathews, NC) using the Fmoc/tBu strategy as previously described35 or manually starting from PAL-PEG polystyrene resin (0.21 mmol/g). For manual synthesis the following steps were undertaken: (a) Fmoc deprotection with 20percent piperidine for 5 min, then 15 min, washing with DMF 5.x.; (b) coupling of the Fmoc amino acid (5 equiv) in the presence of HBTU in DMF (4.9 equiv) and iPr2NEt (10 equiv) for 1 h and washing with DMF 5.x.. For coupling of Fmoc-Pra (1.5 equiv) and Fmoc-N3Ala (1.5 equiv), 1.45 equiv of HBTU and 4.5 equiv of iPr2NEt were used. The progress of the acylation step was monitored by the Kaiser test. A minimum amount of DMF was used for dissolution of the Fmoc amino acid. The resulting peptides were cleaved from the resin with simultaneous side chain protecting group removal by treatment with either TFA/iPr3SiH/DODT/H2O (v/v/v/v; 94/1/2.5/2.5), or with TFA/iPr3SiH/H2O (v/v/v; 95/2.5/2.5) for 2 h at room temperature. Crude peptides were precipitated and triturated with cold diethyl ether, isolated (centrifugation), dissolved in 20percent acetonitrile (aq) containing 0.1percent TFA and lyophilized. Analytical RP-HPLC was performed using a Dionex P680 (flow rate of 1 mL/min), or Dionex Ultimate U3000 system (flow rate of 0.5 mL/min or 0.2 mL/min) using Waters XTerra.(R). column (MS C18, 150 mm .x. 4.6 mm; 5 mum) or, Phenomenex Aqua column (C18, 250 mm .x. 4.6 mm; 5mu), or Phenomenex, Gemini column (C18, 50 mm .x. 2.0 mm, 5mu), using gradient systems as indicated in the Supplementary data. The solvent system used was A (0.1percent TFA in H2O) and B (0.1percent TFA in acetonitrile) with detection at 210 nm, 254 nm, and 280 nm****. The ratio of products was determined by integration of spectra recorded at 210 nm. Peptide masses were confirmed by an inline Thermo Finnegan MSQ mass spectrometer using ESI in the positive mode. When appropriate, a Bruker micrOTOF-Q II mass spectrometer was used for ESI-MS analysis (positive mode). Infrared spectra were obtained using a Perkin Elmer Spectrum One Fourier Transform infrared spectrometer with a universal ATR sampling accessory. Peptide purification was performed using a Waters 600E or Dionex Ultimate U3000 system using a Waters XTerra.(R). column (C18, 300 mm .x. 19 mm; 10 mum), or Phenomenex Gemini C18, 250 mm .x. 10 mm; 5 mum 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 three times from 10 mM aq HCl.

References: [1]Bioorganic and Medicinal Chemistry,2012,vol. 20,p. 2661 - 2668.

10
[ 35661-39-3 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 198561-07-8 ]
[ 684270-46-0 ]
C₈₅H₁₁₆N₁₅O₁₇Pol [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: Fmoc SPPS was performed on a Liberty Microwave Peptide Synthesiser (CEM Corporation, Mathews, NC) using the Fmoc/tBu strategy as previously described35 or manually starting from PAL-PEG polystyrene resin (0.21 mmol/g). For manual synthesis the following steps were undertaken: (a) Fmoc deprotection with 20percent piperidine for 5 min, then 15 min, washing with DMF 5.x.; (b) coupling of the Fmoc amino acid (5 equiv) in the presence of HBTU in DMF (4.9 equiv) and iPr2NEt (10 equiv) for 1 h and washing with DMF 5.x.. For coupling of Fmoc-Pra (1.5 equiv) and Fmoc-N3Ala (1.5 equiv), 1.45 equiv of HBTU and 4.5 equiv of iPr2NEt were used. The progress of the acylation step was monitored by the Kaiser test. A minimum amount of DMF was used for dissolution of the Fmoc amino acid. The resulting peptides were cleaved from the resin with simultaneous side chain protecting group removal by treatment with either TFA/iPr3SiH/DODT/H2O (v/v/v/v; 94/1/2.5/2.5), or with TFA/iPr3SiH/H2O (v/v/v; 95/2.5/2.5) for 2 h at room temperature. Crude peptides were precipitated and triturated with cold diethyl ether, isolated (centrifugation), dissolved in 20percent acetonitrile (aq) containing 0.1percent TFA and lyophilized. Analytical RP-HPLC was performed using a Dionex P680 (flow rate of 1 mL/min), or Dionex Ultimate U3000 system (flow rate of 0.5 mL/min or 0.2 mL/min) using Waters XTerra.(R). column (MS C18, 150 mm .x. 4.6 mm; 5 mum) or, Phenomenex Aqua column (C18, 250 mm .x. 4.6 mm; 5mu), or Phenomenex, Gemini column (C18, 50 mm .x. 2.0 mm, 5mu), using gradient systems as indicated in the Supplementary data. The solvent system used was A (0.1percent TFA in H2O) and B (0.1percent TFA in acetonitrile) with detection at 210 nm, 254 nm, and 280 nm****. The ratio of products was determined by integration of spectra recorded at 210 nm. Peptide masses were confirmed by an inline Thermo Finnegan MSQ mass spectrometer using ESI in the positive mode. When appropriate, a Bruker micrOTOF-Q II mass spectrometer was used for ESI-MS analysis (positive mode). Infrared spectra were obtained using a Perkin Elmer Spectrum One Fourier Transform infrared spectrometer with a universal ATR sampling accessory. Peptide purification was performed using a Waters 600E or Dionex Ultimate U3000 system using a Waters XTerra.(R). column (C18, 300 mm .x. 19 mm; 10 mum), or Phenomenex Gemini C18, 250 mm .x. 10 mm; 5 mum 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 three times from 10 mM aq HCl.

References: [1]Bioorganic and Medicinal Chemistry,2012,vol. 20,p. 2661 - 2668.

11
[ 35661-39-3 ]
C₂₄H₂₉NO₆ [ No CAS ]
[ 122889-11-6 ]
[ 71989-23-6 ]
(3S,7S,10S,13S)-3-((3aR,6S,6aR)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-5-yl)-13-(benzyloxymethyl)-10-sec-butyl-7-methyl-5,8,11-trioxo-1-phenyl-2,6,9,12-tetraazatetradecan-14-oic acid [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
79%		General procedure: The peptides were synthesized on an activated [44] 2-chlorotrityl chloride resin (1?g) which had been swelled in dry DCM for 30?min. The first Fmoc amino acid (4?equiv) was coupled to the resin manually using dry DCM (10?mL) and DIPEA (6?equiv) for 2?h under a N2 atmosphere. Resin substitution was then determined using the Fmoc UV assay. On 0.1?mM scale subsequent amino acids were also coupled manually using amino acid (0.20?mM, 2.5?mL), DIPEA (1?mM, 1.0?mL) and HBTU (0.50?mM, 1.0?mL) in DMF. The Fmoc group of amino acid was removed using 20percent piperidine?DMF (3?×?10?mL) for 30?min and the next amino acid and sugar amino acid 1a/b were coupled on resin using the same condition. The excess reagents were washed with DMF (2?×?7?mL) and DCM (2?×?7?mL). Cleavage from resin was performed manually, using a cleavage mixture of TFA?DCM [5:95percent (v/v), 3?×?10?mL] for 30?min. The crude compound was then purified using semi-preparative HPLC. All compounds were obtained in good yields.

References: [1]European Journal of Medicinal Chemistry,2013,vol. 60,p. 144 - 154.

12
[ 35661-39-3 ]
C₂₂H₃₁NO₈ [ No CAS ]
[ 122889-11-6 ]
[ 71989-23-6 ]
(2S)-2-((2S,3S)-2-((2S)-2-((3S)-3-amino-3-((3aR,6S,6aR)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-5-yl)propanamido)propanamido)-3-methylpentanamido)-3-(benzyloxy)propanoic acid [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
80%		General procedure: The peptides were synthesized on an activated [44] 2-chlorotrityl chloride resin (1?g) which had been swelled in dry DCM for 30?min. The first Fmoc amino acid (4?equiv) was coupled to the resin manually using dry DCM (10?mL) and DIPEA (6?equiv) for 2?h under a N2 atmosphere. Resin substitution was then determined using the Fmoc UV assay. On 0.1?mM scale subsequent amino acids were also coupled manually using amino acid (0.20?mM, 2.5?mL), DIPEA (1?mM, 1.0?mL) and HBTU (0.50?mM, 1.0?mL) in DMF. The Fmoc group of amino acid was removed using 20percent piperidine?DMF (3?×?10?mL) for 30?min and the next amino acid and sugar amino acid 1a/b were coupled on resin using the same condition. The excess reagents were washed with DMF (2?×?7?mL) and DCM (2?×?7?mL). Cleavage from resin was performed manually, using a cleavage mixture of TFA?DCM [5:95percent (v/v), 3?×?10?mL] for 30?min. The crude compound was then purified using semi-preparative HPLC. All compounds were obtained in good yields.

References: [1]European Journal of Medicinal Chemistry,2013,vol. 60,p. 144 - 154.

13
[ 35661-39-3 ]
[ 1356004-85-7 ]
[ 71989-26-9 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
[ 1421510-96-4 ]

References: [1]Chemical Communications,2013,vol. 49,p. 4540 - 4542.

14
[ 35661-39-3 ]
[ 1356004-85-7 ]
[ 71989-18-9 ]
[ 71989-26-9 ]
[ 198561-07-8 ]
[ 1421510-90-8 ]

References: [1]Chemical Communications,2013,vol. 49,p. 4540 - 4542.

15
[ 35661-39-3 ]
[ 1427040-55-8 ]
[ 122889-11-6 ]
[ 71989-23-6 ]
[ 122350-52-1 ]
(6S,9S,12S,15S)-6-{(S)-3-amino-3-[(3aR,5R,6S,6aR)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-5-yl]propanamido}-15-(benzyloxymethyl)-12-sec-butyl-9-methyl-3,7,10,13-tetraoxo-1-phenyl-2-oxa-8,11,14-triazahexadecan-16-oic acid [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
64%		The peptide 4 was synthesized manually on an activated 2-chlorotrityl chloride resin (1 g) which had been swelled in dry DCM for 30 min. The first amino acid Fmoc-Ser-OH was coupled to the resin using dry DCM (10 mL) and DIPEA (6.65 mmol) for 2 h under a N2 atmosphere. Resin substitution was 0.6 mol g?1 as determined by the Fmoc UV assay. The Fmoc group of serine was removed using 20 percent piperidine in DMF (3 × 10 mL) for30 min. Subsequently, amino acids Fmoc-Ile-OH, Fmoc-Ala-OH,and Fmoc-Glu-OH (0.20 mM) were coupled using DIPEA (1 mM) and HCTU (0.50 mM) in DMF. The Fmoc group of glutamic acid was removed using 20 percent piperidine in DMF (3 ×10 mL) for 30 min and finally sugar amino acid 1 was coupled using DIPEA (1 mM) and HCTU (0.50 mM) in DMF. Standardwashing procedures were used. Cleavage from the resin was performed, using a cleavage mixture of 5 percent TFA in DCM (3 ×10 mL)for 30 min. The crude compound was then purified usingsemi-preparative HPLC on a Shimadzu Instrument LC-8A (AceC18 150 mm × 21.2 mm × 5 mm) with an UV/VIS detector SPD-M20A (215nmand 254 nm) and automated fraction collector FRC-10a with 15mLmin?1 flow rate and two buffer system waterand MeOH containing 0.1 percent HCOOH with method RP-HPLC:5 percent MeOH /95 percent H2O/0.1 percent HCOOH to 95 percent MeOH /5 percentH2O/0.1 percent HCOOH in 35 min. Compound 4 was obtained in 64 percent yield as a white solid, mp 171 °C.

References: [1]South African Journal of Chemistry,2014,vol. 67,p. 80 - 84.

16
[ 1026023-54-0 ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 556-08-1 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 109425-51-6 ]
[ 116821-47-7 ]
[ 198561-07-8 ]
[ 334918-39-7 ]
C₁₂₈H₂₁₈N₅₀O₃₆ [ No CAS ]

References: [1]Organic and Biomolecular Chemistry,2015,vol. 13,p. 5273 - 5278.

17
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 67436-13-9 ]
[ 198561-07-8 ]
Pra-TLPSTCGAS-CONH2 [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		All peptides were synthesized on a 0.2 mmol scale using manual Fmoc-SPPS chemistry under flow using a 3 minute cycle for each amino acid. Specifically, all reagents and solvents are delivered to a stainless steel reactor containing resins at a constant flow rate using HPLC pump; temperature of the reactor was maintained at 60 °C during the synthesis using water bath. Procedure for each amino acid coupling cycle included a 30 second coupling with 1 mmol Fmoc-protected amino acid, 1 mmol HBTU, and 500 of diisopropyl ethyl amine (DIEA) in 2.5 mL of DMF at a flow rate of 6 mL/min (note that for coupling of cysteine and tryptophan, 190 of DIEA was used to prevent racemization); 1 minute wash with DMF at a flow rate of 20 mL/min; 20 second deprotection with 50percent (v/v) piperidine in DMF at a flow rate of 20 mL/min; and 1 minute wash with DMF at a flow rate was 20 mL/min. After completion of the stepwise SPPS, the resin was washed thoroughly with DCM and dried under vacuum. The peptide is simultaneously cleaved from the resin and side-chain deprotected by treatment with 2.5percent (v/v) water, 2.5percent (v/v) 1 ,2- ethanedithiol (EDT), and 1percent (v/v) triisoproprylsilane in neat trifluoroacetic acid (TFA) for 2 hours at room temperature. The resulting solution containing peptide was evaporated by blowing a stream of nitrogen gas over its surface for 15 minutes, then triturated and washed with cold diethyl ether three times. The obtained gummy-like solid was dissolved in 50percent H20: 50percent acetonitrile containing 0.1percent TFA and lyophilized. These same solvent compositions were used in majority of experiments and will be referred to as A: 0.1percent TFA in H20 and B: 0.1percent TFA in acetonitrile. c. Peptide Purification The crude peptide was dissolved in 95percent A: 5percent B with 6 M guanidinium hydrochloride and purified by semi-preparative RP-HPLC (Agilent Zorbax SB C18 column: 21.2 x 250 mm, 7 mutaueta, linear gradient: 5-50percent B over 90 min, flow rate: 5 mL/min). 1 of each HPLC fraction was mixed with 1 mu^ of alpha-cyano-4-hydroxycinnamic acid (CHCA) matrix in 75percent A: 25percent B, spotted with MALDI, and checked for fractions with desired molecular mass. The purity of fractions was confirmed by analytical RP-HPLC (Agilent Zorbax SB C3 column: 2.1 x 150 mm, 5 muiotaeta, gradient: 0-2 minutes 5percent B, 2-11 minutes 5- 65percent B, 11-12 minutes 65percent B, flow rate: 0.8 mL/min). HPLC fractions containing only product materials were confirmed by LC-MS analysis, combined, and then lyophilized. Peptides synthesized using fast flow-based SPPS and purified by RP-HPLC are listed in Table SI .

References: [1]Patent: WO2015/175941,2015,A1 .Location in patent: Page/Page column 47-48.

18
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
N⁴-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-N²-(9-fluorenylmethylcarbonyl)asparagine [ No CAS ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 109425-51-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
KCNTATCATQRLANFLVHSS-(α-propargylglycinyl)-NFGPILPPTNVGS-(N⁴-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)asparaginyl)-TY-NH₂ [ No CAS ]