132622-66-3

Basic information

• Product Name: (S)-(+)-N-BOC-4-AMINO-L-PROLINE, 97
• Synonyms: (S)-(+)-N-BOC-4-AMINO-L-PROLINE, 97;(S)-(+)-N-BOC-4-AMINO-L-PROLINE, 97%;CIS-1-BOC-4-AMINO-L-PROLINE ;cis-4-Amino-1-Boc-2-pyrrolidinecarboxylic acid;(2S,4S)-4-Amino-pyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester;(2S,4S)-4-amino-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic acid;2S,4S)-4-aMino-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic a;(2S,4S)-4-Amino-1,2-pyrrolidinedicarboxylic acid 1-(tert-butyl) ester
• CAS NO: 132622-66-3
• Molecular Formula: C₁₀H₁₈N₂O₄
• Molecular Weight: 230.26092
• Product Categories: pharmacetical
• Mol File: 132622-66-3.mol

Chemical Properties

• Melting Point: >266 °C(lit.)
• Boiling Point: 371.1 °C at 760 mmHg
• Flash Point: 178.2 °C
• Appearance: /
• Density: 1.232
• Vapor Pressure: 1.59E-06mmHg at 25°C
• Refractive Index: 1.516
• Storage Temp.: 2-8°C(protect from light)
• PKA: 3.65±0.20(Predicted)
• CAS DataBase Reference: (S)-(+)-N-BOC-4-AMINO-L-PROLINE, 97(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-(+)-N-BOC-4-AMINO-L-PROLINE, 97(132622-66-3)
• EPA Substance Registry System: (S)-(+)-N-BOC-4-AMINO-L-PROLINE, 97(132622-66-3)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 132622-66-3(Hazardous Substances Data)

Usage

Uses

also available as trans isomer, see 1-00971

InChI:InChI=1/C10H18N2O4/c1-10(2,3)16-9(15)12-5-6(11)4-7(12)8(13)14/h6-7H,4-5,11H2,1-3H3,(H,13,14)/t6-,7-/m1/s1

Upstream product

• 74844-91-0 1-tert-butyl 2-methyl (2S,4R)-4-hydroxy-1,2-pyrrolidinedicarboxylate 
• 24424-99-5 di-tert-butyl dicarbonate 
• 1499-56-5 (R)-4-hydroxy-L-proline ethyl ester 
• 84520-68-3 N-tert-butoxycarbonyl-cis-4-azido-L-proline methyl ester 
• 84520-67-2 (2S,4R)-4-(methylsulfonyloxy)pyrrolidine-1,2-dicarboxylic acid 1-tert-butylester-2-methylester 
• 174148-03-9 (2S,4S)-4-(9H-fluoren-9-ylmethoxycarbonylamino)-pyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester 
• 132622-65-2 (4S)-1-(tert-butoxycarbonyl)-4-azido-L-proline 
• 132622-68-5 (2S,4R)-4-azido-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic acid 
• 121148-01-4 (2S,4S)-4-amino-pyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester 2-methyl ester 
• 132623-03-1 (2S,4S)-4-azido-pyrrolidin-1,2-dicarboxylic acid-1-tert-butyl ester-2-ethyl ester 
• 89813-47-8 N-(tert-butoxycarbonyl)-(2S,4R)-4-hydroxyproline benzyl ester 
• 865295-35-8 2-benzyl 1-(tert-butyl) (2S,4R)-4-((methylsulfonyl)oxy)pyrrolidine-1,2-dicarboxylate 
• 874162-96-6 (2S,4S)-2-benzyl 1-tert-butyl 4-azidopyrrolidine-1,2-dicarboxylate 
• 1217446-43-9 (2S,4S)-4-aminopyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester 2-methyl ester hydrochloride 

Downstream Products

• 913979-48-3 C₁₇H₂₃FN₂O₄ 
• 174148-03-9 (2S,4S)-4-(9H-fluoren-9-ylmethoxycarbonylamino)-pyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester 
• 132622-67-4 (4S)-1-(tert-butoxycarbonyl)-4-<<<(p-toluenesulfonyl)imino>aminomethyl>amino>-L-proline 
• 874163-08-3 3(R)-[(4(S)-((4-azido-2-hydroxy-5-iodobenzoyl)amino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-07-2 3(R)-[(4(S)-((4-azido-2-hydroxybenzoyl)amino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-06-1 3(R)-[(4(S)-((4-azidobenzoyl)amino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-02-7 methyl 3(R)-[(4(S)-(4-benzyloxycarbonylamino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetate 
• 874163-04-9 3(R)-[(4(S)-(4-benzyloxycarbonylamino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874162-99-9 (2S,4S)-4-(((benzyloxy)carbonyl)amino)-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic acid 

Relevant articles and documents

Superior HIV-1 TAR Binders with Conformationally Constrained R52 Arginine Mimics in the Tat(48–57) Peptide

We report a 100-fold increase in binding affinity of the Tat(48–57) peptide to HIV-1 transcriptional activator-responsive element (TAR) RNA by replacing Arg52, an essential and critical residue for Tat's specific binding, with (2S,4S)-4-guanidinoproline. The resulting αTat1M peptide is a far superior binder than γTat1M, a peptide containing another conformationally constrained arginine mimic, (2S,4S)-4-amino-N-(3-guanidinopropyl)proline, or even the control Tat peptide (CtrlTat) itself. Our observations are supported by circular dichroism (CD), isothermal titration calorimetry (ITC), gel electrophoresis and UV spectroscopy studies. Molecular dynamics simulations suggest increased interactions between the more compact αTat1M and TAR RNA, relative to CtrlTat. The CD signature of the RNA itself remains largely unchanged upon binding of the peptides. The Tat mimetics further have better cell uptake properties than the control Tat peptide, thus increasing their potential application as specific TAR-binding molecules.

Discovery of subnanomolar arginine-glycine-aspartate-based αvβ3/αvβ5 integrin binders embedding 4-aminoproline residues

The embodiment of 4-aminoproline residues (Amp) into the arginine-glycine-aspartate (RGD) sequence led to the discovery of a novel class of high-affinity αvβ3/αvβ 5 integrin binders [IC50h(αvβ 3) 0.03-5.12 nM; IC50h(αvβ 5) 0.88-154 nM]. A total of eight cyclopeptides of type cyclo-[-Arg-Gly-Asp-Amp-], 5-12, were assembled by a standard solid-phase peptide synthesis protocol that involved the C2-carboxyl and C4-amino functionalities of the proline scaffolds, leaving the Nα- nuclear site untouched. Functionalization of this vacant proline site with either alkyl or acyl substituents proved feasible, with significant benefit to the integrin binding capabilities of the ligands. Notably, six out of eight cyclopeptide inhibitors, 5-7 and 9-11, showed moderate yet significant selectivity toward the αvβ3 receptor. The three-dimensional structure in water was determined by NMR techniques and molecular dynamics calculations. Docking studies to the X-ray crystal structure of the extracellular segment of integrin αvβ3 complexed with reference compound 1 were also performed on selected analogues to highlight the structural features required for potent ligand binding affinity.

DIPEPTIDYL PEPTIDASE-IV INHIBITORS

The present invention relates generally to pyrrolidine and thiazolidine DPP-IV inhibitor compounds. The present invention also provides synthetic methods for preparation of such compounds, methods of inhibiting DPP-IV using such compounds and pharmaceutical formulations containing them for treatment of DPP-IV mediated diseases, in particular, Type-2 diabetes.

ANTIVIRAL COMPOUNDS

The invention is related to phosphorus substituted anti-viral inhibitory compounds, compositions containing such compounds, and therapeutic methods that include the administration of such compounds, as well as to processes and intermediates useful for preparing such compounds.

Design and synthesis of photoaffinity-labeling ligands of the L-prolyl-L-leucylglycinamide binding site involved in the allosteric modulation of the dopamine receptor

Pro-Leu-Gly-NH2 (PLG), in addition to its endocrine effects, possesses the ability to modulate dopamine 02 receptors within the central nervous system. However, the precise binding site of PLG is unknown. Potential photoaffinity-labeling ligand

Engineering of a 129-Residue Tripod Protein by Chemoselective Ligation of Proline-II Helices

A 129-residue tripod protein was designed, synthesized, and biophysically characterized.This receptor-adhesive modular protein contained three 30-residue proline-II helices linked to a 9-residue proline-II helix through thioether bonds.Coupling of 6-maleimidohexanoic acid succinimido ester to cis-Nα-Boc-4-amino-L-proline furnished in 77percent yield the maleimido acid cis-N-Boc-4-(6-maleimidohexanamido)-L-proline (Boc-Prm), which was used in the solid-phase synthesis of the linker peptide CH3-CO-Pro3-Prm3-Pro3-NH2.The leg peptide, the 40-residue thiol Gly-Arg-Gly-Asp-Ser-Pro-Gly-Tyr-Gly-Pro30-Cys-NH2, was also made by solid-phase synthesis.The tripod protein was prepared by Michael addition of the thiol groups of three leg peptides to the three maleimide groups of the linker peptide.By 13C NMR spectrometry, the linker peptide was a proline-II helix, as indicated by the presence of only trans Pro-Pro resonances for its β and γ carbons.By circular dichroic spectroscopy, the model peptide CH3-CO-Pro9-NH2, the linker peptide, the leg peptide, and the tripod proteinn each contained substantial proline-II helix, as indicated by a strong negative band at 205 nm and a weak positive band at 226 nm.Since the Pro30 proline-II helix of each leg is about 93 Angstroem long, two Arg-Gly-Asp sites on different legs of the tripod protein could be as much as ca. 250 Angstroem apart.

Chimeric amino acid analogues

A chimeric amino acid analogue is provided suitable for incorporating into peptides which compound is represented by Formula 1: STR1 where P1 is preferably an amine protecting agent, and P2 and P3 are preferably amine or guanidine protecting agents. X can be OH, halide, or preferably an activating group suitable for conjugating the compound of Formula 1 to a peptide by conventional means, and m and n are 0-1 and 0-2 respectively. Peptides containing the chimeric amino acid analog are provided and include a platelet-aggregation inhibitor represented by where Aaa1 is Gly or H, Cpdl is the compound of Formula 1 which has been deprotected and Aaa2 is a hydrophobic amino acid preferably Val.

Conformationally Restricted Arginine Analogues

We report the practical synthesis and structural characterization of a set of conformationally constrained protected arginine analogues.These enantiomerically pure analogues have the general structure 1 and are prepared in seven to eight steps from the co