Fmoc-Ile-OH | Carboxylic Acids

Structure of Fmoc-Ile-OH
CAS No.: 71989-23-6

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Synonyms: Fmoc-L-isoleucine

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Quality Control of [ 71989-23-6 ] Purity: 98% SDS Specification

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Product Details of [ 71989-23-6 ]

CAS No. :	71989-23-6
Formula :	C₂₁H₂₃NO₄
M.W :	353.41
SMILES Code :	CC[C@H](C)[C@@H](C(O)=O)NC(OCC1C2=CC=CC=C2C3=CC=CC=C13)=O
Synonyms :	Fmoc-L-isoleucine
MDL No. :	MFCD00037125
InChI Key :	QXVFEIPAZSXRGM-DJJJIMSYSA-N
Pubchem ID :	2724629

Safety of [ 71989-23-6 ]

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

Computational Chemistry of [ 71989-23-6 ] Show Less

Physicochemical Properties

Num. heavy atoms	26
Num. arom. heavy atoms	12
Fraction Csp3	0.33
Num. rotatable bonds	8
Num. H-bond acceptors	4.0
Num. H-bond donors	2.0
Molar Refractivity	99.59
TPSA ? Topological Polar Surface Area: Calculated from Ertl P. et al. 2000 J. Med. Chem.	75.63 Å²

Lipophilicity

Log P_o/w (iLOGP)? iLOGP: in-house physics-based method implemented from Daina A et al. 2014 J. Chem. Inf. Model.	2.54
Log P_o/w (XLOGP3)? XLOGP3: Atomistic and knowledge-based method calculated by XLOGP program, version 3.2.2, courtesy of CCBG, Shanghai Institute of Organic Chemistry	4.38
Log P_o/w (WLOGP)? WLOGP: Atomistic method implemented from Wildman SA and Crippen GM. 1999 J. Chem. Inf. Model.	4.02
Log P_o/w (MLOGP)? MLOGP: Topological method implemented from Moriguchi I. et al. 1992 Chem. Pharm. Bull. Moriguchi I. et al. 1994 Chem. Pharm. Bull. Lipinski PA. et al. 2001 Adv. Drug. Deliv. Rev.	3.0
Log P_o/w (SILICOS-IT)? SILICOS-IT: Hybrid fragmental/topological method calculated by FILTER-IT program, version 1.0.2, courtesy of SILICOS-IT, http://www.silicos-it.com	3.55
Consensus Log P_o/w? Consensus Log P_o/w: Average of all five predictions	3.5

Water Solubility

Log S (ESOL):? ESOL: Topological method implemented from Delaney JS. 2004 J. Chem. Inf. Model.	-4.6
Solubility	0.00879 mg/ml ; 0.0000249 mol/l
Class? Solubility class: Log S scale Insoluble < -10 < Poorly < -6 < Moderately < -4 < Soluble < -2 Very < 0 < Highly	Moderately soluble
Log S (Ali)? Ali: Topological method implemented from Ali J. et al. 2012 J. Chem. Inf. Model.	-5.68
Solubility	0.000731 mg/ml ; 0.00000207 mol/l
Class? Solubility class: Log S scale Insoluble < -10 < Poorly < -6 < Moderately < -4 < Soluble < -2 Very < 0 < Highly	Moderately soluble
Log S (SILICOS-IT)? SILICOS-IT: Fragmental method calculated by FILTER-IT program, version 1.0.2, courtesy of SILICOS-IT, http://www.silicos-it.com	-5.71
Solubility	0.000689 mg/ml ; 0.00000195 mol/l
Class? Solubility class: Log S scale Insoluble < -10 < Poorly < -6 < Moderately < -4 < Soluble < -2 Very < 0 < Highly	Moderately soluble

Pharmacokinetics

GI absorption? Gatrointestinal absorption: according to the white of the BOILED-Egg	High
BBB permeant? BBB permeation: according to the yolk of the BOILED-Egg	Yes
P-gp substrate? P-glycoprotein substrate: SVM model built on 1033 molecules (training set) and tested on 415 molecules (test set) 10-fold CV: ACC=0.72 / AUC=0.77 External: ACC=0.88 / AUC=0.94	Yes
CYP1A2 inhibitor? Cytochrome P450 1A2 inhibitor: SVM model built on 9145 molecules (training set) and tested on 3000 molecules (test set) 10-fold CV: ACC=0.83 / AUC=0.90 External: ACC=0.84 / AUC=0.91	Yes
CYP2C19 inhibitor? Cytochrome P450 2C19 inhibitor: SVM model built on 9272 molecules (training set) and tested on 3000 molecules (test set) 10-fold CV: ACC=0.80 / AUC=0.86 External: ACC=0.80 / AUC=0.87	Yes
CYP2C9 inhibitor? Cytochrome P450 2C9 inhibitor: SVM model built on 5940 molecules (training set) and tested on 2075 molecules (test set) 10-fold CV: ACC=0.78 / AUC=0.85 External: ACC=0.71 / AUC=0.81	Yes
CYP2D6 inhibitor? Cytochrome P450 2D6 inhibitor: SVM model built on 3664 molecules (training set) and tested on 1068 molecules (test set) 10-fold CV: ACC=0.79 / AUC=0.85 External: ACC=0.81 / AUC=0.87	No
CYP3A4 inhibitor? Cytochrome P450 3A4 inhibitor: SVM model built on 7518 molecules (training set) and tested on 2579 molecules (test set) 10-fold CV: ACC=0.77 / AUC=0.85 External: ACC=0.78 / AUC=0.86	Yes
Log Kp (skin permeation)? Skin permeation: QSPR model implemented from Potts RO and Guy RH. 1992 Pharm. Res.	-5.35 cm/s

Druglikeness

Lipinski? Lipinski (Pfizer) filter: implemented from Lipinski CA. et al. 2001 Adv. Drug Deliv. Rev. MW ≤ 500 MLOGP ≤ 4.15 N or O ≤ 10 NH or OH ≤ 5	0.0
Ghose? Ghose filter: implemented from Ghose AK. et al. 1999 J. Comb. Chem. 160 ≤ MW ≤ 480 -0.4 ≤ WLOGP ≤ 5.6 40 ≤ MR ≤ 130 20 ≤ atoms ≤ 70	None
Veber? Veber (GSK) filter: implemented from Veber DF. et al. 2002 J. Med. Chem. Rotatable bonds ≤ 10 TPSA ≤ 140	0.0
Egan? Egan (Pharmacia) filter: implemented from Egan WJ. et al. 2000 J. Med. Chem. WLOGP ≤ 5.88 TPSA ≤ 131.6	0.0
Muegge? Muegge (Bayer) filter: implemented from Muegge I. et al. 2001 J. Med. Chem. 200 ≤ MW ≤ 600 -2 ≤ XLOGP ≤ 5 TPSA ≤ 150 Num. rings ≤ 7 Num. carbon > 4 Num. heteroatoms > 1 Num. rotatable bonds ≤ 15 H-bond acc. ≤ 10 H-bond don. ≤ 5	0.0
Bioavailability Score? Abbott Bioavailability Score: Probability of F > 10% in rat implemented from Martin YC. 2005 J. Med. Chem.	0.56

Medicinal Chemistry

PAINS? Pan Assay Interference Structures: implemented from Baell JB. & Holloway GA. 2010 J. Med. Chem.	0.0 alert
Brenk? Structural Alert: implemented from Brenk R. et al. 2008 ChemMedChem	0.0 alert: heavy_metal
Leadlikeness? Leadlikeness: implemented from Teague SJ. 1999 Angew. Chem. Int. Ed. 250 ≤ MW ≤ 350 XLOGP ≤ 3.5 Num. rotatable bonds ≤ 7	No; 1 violation:MW<3.0
Synthetic accessibility? Synthetic accessibility score: from 1 (very easy) to 10 (very difficult) based on 1024 fragmental contributions (FP2) modulated by size and complexity penaties, trained on 12'782'590 molecules and tested on 40 external molecules (r² = 0.94)	4.05

Application In Synthesis of [ 71989-23-6 ]

* 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.

Downstream synthetic route of [ 71989-23-6 ]

[ 71989-23-6 ] Synthesis Path-Downstream 1~41

1
[ 29022-11-5 ]
[ 35661-40-6 ]
[ 108-24-7 ]
[ 71989-23-6 ]
[ 198561-07-8 ]
Ac-Ile-Asp-Phe-Gly-OH [ No CAS ]

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

2
[ 159610-89-6 ]
Nα-Fmoc-Arg(NG-pbf)-Rink amide resin [ No CAS ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 108-24-7 ]
[ 71989-23-6 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 75932-02-4 ]
[ 198561-07-8 ]
[ 1217266-32-4 ]

References: [1]European Journal of Organic Chemistry,2010,p. 446 - 457.

3
Nα-Fmoc-Arg(NG-pbf)-Rink amide resin [ No CAS ]
[ 1097192-04-5 ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 108-24-7 ]
[ 71989-23-6 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 75932-02-4 ]
[ 198561-07-8 ]
[ 1217266-30-2 ]

References: [1]European Journal of Organic Chemistry,2010,p. 446 - 457.

4
Nα-Fmoc-Arg(NG-pbf)-Rink amide resin [ No CAS ]
[ 1097192-04-5 ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 108-24-7 ]
[ 71989-23-6 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 75932-02-4 ]
[ 198561-07-8 ]
[ 1217266-28-8 ]

References: [1]European Journal of Organic Chemistry,2010,p. 446 - 457.

5
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.

6
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 108-24-7 ]
[ 71989-23-6 ]
[ 71989-16-7 ]
[ 91000-69-0 ]
[ 198561-07-8 ]
C₅₇H₉₃N₁₇O₂₂ [ No CAS ]

References: [1]Organic Letters,2011,vol. 13,p. 5604 - 5607.

7
[ 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.

8
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 152338-45-9 ]
[ 185031-78-1 ]
[ 122889-11-6 ]
[ 71989-31-6 ]
[ 71989-23-6 ]
[ 117872-75-0 ]
[ 136050-67-4 ]
GTCNTPGCTCSWPVCQIPGLGPLCGETCVG cyclic (3->15),(8->24),(10->28)-tris(disulfide) [ No CAS ]

References: [1]Angewandte Chemie - International Edition,2012,vol. 51,p. 5620 - 5624.

9
[ 258332-56-8 ]
C₂₉H₃₀NO₄Pol [ No CAS ]
[ 71989-31-6 ]
[ 71989-23-6 ]
[ 105047-45-8 ]
[ 198561-07-8 ]
C₄₄H₇₀N₈O₁₀ [ No CAS ]

References: [1]ChemMedChem,2013,vol. 8,p. 75 - 81.

10
[ 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.

11
[ 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.

12
Fmoc-Asp(otBu)-Wang resin [ No CAS ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 120791-76-6 ]
[ 198561-07-8 ]
[ 684270-46-0 ]
C₁₃₅H₁₈₂N₁₈O₂₃S₃ [ No CAS ]

References: [1]Organic and Biomolecular Chemistry,2012,vol. 10,p. 7753 - 7762.

13
[ 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.

14
Fmoc-alanine-Wang-resin [ No CAS ]
[ 122889-11-6 ]
[ 108-24-7 ]
[ 71989-23-6 ]
N-acetyl-L-isoleucyl-L-(OBn)seryl-L-alanine [ No CAS ]

References: [1]RSC Advances,2015,vol. 5,p. 22431 - 22448.

15
Fmoc-Leu-Wang resin [ No CAS ]
[ 214750-72-8 ]
[ 258332-56-8 ]
[ 71989-31-6 ]
[ 71989-23-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
H-propargyl-Gly-N-Me-Arg-Lys-Pro-N-homo-Tyr-Ile-Leu-OH [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		The solid phase peptide synthesis (SPPS) was performed using a microwave assisted protocol (Discover microwave oven, CEMCorp.) starting from Fmoc-Leu-Wang resin. The reactions were carried out in a silanized glass tube loosely sealed with a silicon septum. Remark: the development of overpressure was avoided by using DMF as the solvent and intermittent cooling in an ethanol-ice bath. The amino acids were incorporated as their commercially available derivatives in the following order: Fmoc-Ile-OH, Fmoc-N-homo-Tyr(tBu)-OH (synthesized according to ref. 18), Fmoc-Pro-OH, Fmoc-Arg(Pbf)-OH, Fmoc-N-Me-Arg(Mtr)-OH and Fmoc-propargyl-Gly-OH. Elongation of the peptide chain was performedby repetitive cycles of Fmoc deprotection and subsequent couplings of the amino acid. Fmoc deprotection was performed by treating the resin with 25% piperidine in DMF (microwave irradiation: 7 5 s, 100 W), followed by washings with DMF (5). In between each irradiation step, cooling of the reaction mixture to a temperature of 10 C was achieved by sufficient agitation in an ethanol-ice bath. Peptide couplings of Fmoc-Ile-OH, Fmoc-Arg(Pbf)-OH and Fmoc-N-Me-Arg(Mtr)-OH were performed employing 5 equiv of each Fmoc-AA/PyBOP/DIPEA and 7.5 equiv 1-hydroxybenzotriazole (HOBt), dissolved in a minimum amount of DMF (irradiation: 20 10 s, 50W and intermittent cooling). Fmoc-N-homo-Tyr(tBu)-OH (3 equiv) was coupled with 3 equiv PyBOP/DIPEA and 4.5 equiv HOBt in DMF. Fmoc-Pro-OH (5 equiv)and Fmoc-propargyl-Gly-OH (5 equiv) were subjected to a double coupling with HATU (5 equiv) and DIPEA (10 equiv) in DMF. After the last acylation step, the N-terminal Fmoc-residue was deprotected, the resin was 10 rinsed with CH2Cl2 and dried in vacuo. The cleavage from the resin was performed using a mixture of trifluoroacetic acid (TFA)/phenol/H2O/triisopropylsilane (TIS) 88:6:4:2 for 4 h, followed by a filtration of the resin. After evaporation of the solvent in vacuo and precipitation in t-butylmethylether, the crude peptides were purified using preparative RP-HPLC (Agilent 1100 preparative series, column Zorbax Eclipse XDB-C8, 21.2 mm, 150 mm, 5 lm particles, flow rate 10 mL/min) with the solvent system 3-35% acetonitrile in water (0.1% HCO2H) in a linear gradient over 18.0 min, tR: 10.5 min. After the separation, the peptide was lyophilized and peptide purity and identity were assessed by analytical HPLC (Agilent 1100 analytical series, equipped with QuatPump and VWD detector; column ZorbaxEclipse XDB-C8 analytical column, 4.6 mm, 150 mm, 5 lm, flow rate 0.5 mL/min) coupled to a Bruker Esquire 2000 mass detector equipped with an ESI-trap. ESI-TOF high mass accuracy and resolution experiments were performed on a BRUKER maXis MS (BrukerDaltonics, Bremen) in the laboratories of the Chair of OrganicChemistry (Prof. Dr. Rik Tykwinski), Department of Pharmacy and Chemistry, Friedrich-Alexander University of Erlangen Nuremberg. Purity: solvent system 1: 10-55% methanol in water (0.1% HCO2H)in a linear gradient over 18 min, tR = 14.6 min (>99 %); solvent system 2: 3-40% acetonitrile in water (0.1% HCO2H) in a linear gradient over 26 min, tR = 15.9 min (>99%). ESI-MS: m/z calcd:940.6, found: 940.6 [M+H]+; HR-ESI-TOF: [M+H]+ calcd forC45H74N13O9: 940.5732, found: 940.5724.

References: [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 4026 - 4033.

16
trityl chloride polystyrene resin [ No CAS ]
[ 1240507-79-2 ]
[ 35737-10-1 ]
[ 71989-23-6 ]
[ 84000-07-7 ]
[ 77128-73-5 ]
C₆₁H₈₂N₅O₁₀PolSi [ No CAS ]

References: [1]Chemistry - A European Journal,2015,vol. 21,p. 18417 - 18430.

17
trityl chloride polystyrene resin [ No CAS ]
[ 1240507-79-2 ]
[ 35737-10-1 ]
[ 71989-23-6 ]
[ 77128-73-5 ]
[ 103478-58-6 ]
C₆₃H₈₆N₅O₁₀PolSi [ No CAS ]

References: [1]Chemistry - A European Journal,2015,vol. 21,p. 18417 - 18430.

18
trityl chloride polystyrene resin [ No CAS ]
[ 1240507-79-2 ]
[ 35737-10-1 ]
[ 103478-62-2 ]
[ 71989-23-6 ]
[ 77128-73-5 ]
C₆₄H₈₈N₅O₁₀PolSi [ No CAS ]

References: [1]Chemistry - A European Journal,2015,vol. 21,p. 18417 - 18430.

19
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 104091-09-0 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 73731-37-0 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 77128-73-5 ]
[ 91000-69-0 ]
[ 116611-64-4 ]
C₁₅₀H₂₂₈N₄₀O₄₅ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: tGLP-1 and its analogues 2?13 were all synthesized using general solid-phase peptide synthesis of N-Fmoc/tBu chemistry. 63Fmoc Rink Amide-MBHA resin (0.1 mmol) was added to a 25 ml peptide synthetic vessel and swollen with DMF for 40 min. After deprotected by 25percent piperidine in DMF, a solution of Fmoc-AA-OH (0.4 mmol), HATU (0.4 mmol), HoAt (0.4 mmol) and DIPEA (0.8 mmol) in DMF was added to the vessel. After reacted for 1 h, the resin was washed three times with DMF and three times with CH2Cl2, then qualitative ninhydrin testing was performed to monitor whether some free amino groups still existed on the resin ornot. If not, the resin was washed three times with DMF again and repeated the procedures of deprotection and coupling. Forthe coupling of some unnatural amino acids, NMM instead of DIPEA and NMP instead of DMF were used. Besides, the reaction time was prolonged to 4 h. Following the final deprotection of N-terminus, the target peptide was cleaved from resin with Reagent K (TFA/thioanisole/water/phenol/EDT, 82.5:5:5:5:2.5) for 2 h atroom temperature. After filtration, the residue solution was concentrated, precipitated with cold diethyl ether and centrifuged for three times. The residue was dissolved in water and purified by Waters 2545 preparative RP-HPLC system. Sephadex G-25 was used for the further purification to remove some short peptide impurities. The molecular mass of the target peptide was confirmed by MALDI-TOF. The purity of peptide was tested with analytical RP-HPLC, and the conditions were as follows: a linear gradient of 20percent mobile phase A and 80percent mobile phase B to 80percent mobile phase A and 20percent mobile phase B (A: acetonitrile containing 0.1percent TFA; B: H2O containing 0.1percent TFA) in 30 min, at a flow rate of 1 mL/minute with UV detection at 214 nm.

References: [1]Bioorganic and Medicinal Chemistry,2016,vol. 24,p. 1163 - 1170.

20
[ 250695-67-1 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 71989-23-6 ]
[ 73731-37-0 ]
[ 73724-45-5 ]
[ 71989-31-6 ]
[ 125238-99-5 ]
[ 143824-78-6 ]
[ 158599-00-9 ]
N-α-(9-fluorenylmethyloxycarbonyl)-N-γ-tert-butyloxycarbonyl-D-2,4-diaminobutyric acid [ No CAS ]
C₇₇H₁₁₈N₂₀O₁₉ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		1. Peptide synthesis 1.1 General synthetic procedures A general method for the synthesis of the peptidomimetics of the present invention is exemplified in the following. This is to demonstrate the principal concept and does not limit or restrict the present invention in any way. A person skilled in the art is easily able to modify these procedures, especially, but not limited to, choosing a different starting position within the ring system, to still achieve the preparation of the claimed cyclic peptidomimetic compounds of the present invention. Coupling of the first protected amino acid residue to the resin . In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1percent crosslinked; loading: 1.4 mMol/g) was swollen in dry CH2CI2 for 30 min (7 mL CH2CI2 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2CI2/DMF (4/1) (10 mL per g resin) was added. After shaking for 2-4 h at rt the resin was filtered off and washed successively with CH2CI2, DMF, CH2CI2, DMF and CH2CI2. Then a solution of dry CH2CI2/MeOH/DIPEA (17:2:1) was added (10 mL per g resin). After shaking for 3 x 30 min the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2CI2, DMF, CH2CI2, MeOH, CH2CI2, MeOH, CH2CI2 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control. Loading was typically 0.6 - 0.7 mMol/g. The following preloaded resins were prepared: Fmoc-Dab(Boc)-2-chlorotrityl resin, Fmoc-DDab(Boc)-2-chlorotrityl resin, Fmoc-Lys(Boc)-2-chlorotrityl resin, Fmoc- Trp(Boc)-2-chlortrityl resin, Fmoc-Phe-2-chlortrityl resin; Fmoc-Val-2-chlorotrityl resin, Fmoc-Pro-2-chlorotrityl resin, Fmoc-Arg(Pbf)-2-chlorotrityl resin and Fmoc-Glu(iBu)-2- chlorotrityl resin. 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 0.04 mMol of the above resin were placed and the resin was swelled in CH2CI2 and DMF for 15 min, respectively. The following reaction cycles were programmed and carried out: Step Reagent Time 1 CH2CI2, wash and swell (manual) 1 x 3 min 2 DMF, wash and swell 2 x 30 min 3 20percent piperidine/DMF 1 x 5 min and 1 x 15 min 4 DMF, wash 5 x 1 min 5 3.5 eq Fmoc amino acid/3.5 eq HOAt in DMF + 3.5 eq PyBOP/7 eq DIPEA or 3.5 eq DIC 1 x 40 min 6 3.5 eq Fmoc amino acid/DMF + 3.5 eq HATU or PyBOP or HCTU + 7 eq DIPEA 1 x 40 min 7 DMF, wash 5 x 1 min 8 20percent piperidine/DMF 1 x 5 min and 1 x 15 min 9 DMF, wash 5 x 1 min 10 CH2CI2, wash (at the end of the synthesis) 3 x 1 min Steps 5 to 9 are repeated to add each amino-acid residue. After the termination of the synthesis of the fully protected peptide fragment, one of the procedures A - E, as described herein below, was adopted subsequently, depending on which kind of interstrand linkages, as described herein below, were to be formed. Finally, the peptides were purified by preparative reverse phase LC-MS, as described herein below. Procedure A: Cyclization and work up of a backbone cyclized peptide having no interstrand linkage Cleavage, backbone cyclization and deprotection After assembly of the linear peptide, the resin was suspended in 1 mL of 1percent TFA in CH2CI2 (v/v; 0.14 mMol) for 3 minutes. After filtration the filtrate was neutralized with 1 mL of 20percent DI PEA in CH2CI2 (v/v; 1.15 mMol). This procedure was repeated four times to ensure completion of the cleavage. An alternative cleavage method comprises suspension of the resin in lmL of 20percent HFIP in CH2CI2 (v/v; 1.9 mMol) for 30 minutes, filtration and repetition of the procedure. The resin was washed three times with 1 mL of CH2CI2. The CH2CI2 layers containing product were evaporated to dryness. The fully protected linear peptide was solubilised in 8 mL of dry DM F. Then 2 eq of HATU and 2 eq of HOAt in dry DM F (1-2 mL) and 4 eq of DIPEA in dry DM F (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 CH2CI2 and washed three times with 4.5 mL 10percent acetonitrile in water (v/v). The CH2CI2 layer was then evaporated to dryness. To fully deprotect the peptide, 7 mL of cleavage cocktail TFA/DODT/thioanisol/H20 (87.5 :2.5:5:5) or TFA/TIS/H20 (95:2.5 :2.5) were added, and the mixture was kept for 2.5-4 h at room temperature until the reaction was completed. The reaction mixture was evaporated close to dryness, the peptide precipitated with 7 mL of cold Et20/pentane and finally washed 3 times with 4 mL of cold Et20/pentane. Procedures Bl and B2: Cyclization and work up of a backbone cyclized peptide having a disulfide interstrand linkage Bl: Formation of a disulfide interstrand linkage using DMSO After cleavage, backbone cyclization and deprotection of the linear peptide, as described in the corresponding section of procedure A, th...

References: [1]Patent: WO2016/50361,2016,A1 .Location in patent: Page/Page column 75-80; 88.

21
[ 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 ]