122350-59-8

Basic information

• Product Name: N-Fmoc-trans-4-hydroxy-L-proline methyl ester
• Synonyms: N-Fmoc-trans-4-hydroxy-L-proline methyl ester;1,2-Pyrrolidinedicarboxylic acid, 4-hydroxy-, 1-(9H-fluoren-9-ylMethyl) 2-Methyl ester, (2S,4R)-;(2S,4R)-1-((9H-Fluoren-9-yl)Methyl) 2-Methyl 4-hydroxypyrrolidine-1,2-dicarboxylate;Fmoc-Hyp-Ome;(2S,4R)-4-hydroxy-1,2-Pyrrolidinedicarboxylic acid 1-(9H-fluoren-9-ylmethyl) 2-methyl ester;2-methyl 4-hydroxypyrrolidine-1,2-dicarboxylate
• CAS NO: 122350-59-8
• Molecular Formula: C₂₁H₂₁NO₅
• Molecular Weight: 367.399
• Mol File: 122350-59-8.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 539.04°C at 760 mmHg
• Flash Point: 279.801°C
• Appearance: /
• Density: 1.329g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.622
• Storage Temp.: 2-8°C
• CAS DataBase Reference: N-Fmoc-trans-4-hydroxy-L-proline methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N-Fmoc-trans-4-hydroxy-L-proline methyl ester(122350-59-8)
• EPA Substance Registry System: N-Fmoc-trans-4-hydroxy-L-proline methyl ester(122350-59-8)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 122350-59-8(Hazardous Substances Data)

Usage

General Description

N-Fmoc-trans-4-hydroxy-L-proline methyl ester is a chemical compound used in organic synthesis and peptide chemistry. It is a derivative of the amino acid proline, featuring a hydroxy group at the 4th position and a methyl ester group. The N-Fmoc (9-fluorenylmethoxycarbonyl) protecting group is commonly used in peptide synthesis to protect the N-terminal amino group. N-Fmoc-trans-4-hydroxy-L-proline methyl ester can be used as a building block for the synthesis of peptides and proteins, particularly those containing proline residues. It is often used in the preparation of peptide libraries for drug discovery and development.

InChI:InChI=1/C21H21NO5/c1-26-20(24)19-10-13(23)11-22(19)21(25)27-12-18-16-8-4-2-6-14(16)15-7-3-5-9-17(15)18/h2-9,13,18-19,23H,10-12H2,1H3/t13-,19+/m1/s1

Upstream product

• 40216-83-9 L-4-hydroxyproline methyl ester hydrochloride 
• 88744-04-1 (9-fluorenyl)methyl pentafluorophenyl carbonate 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 1499-56-5 (R)-4-hydroxy-L-proline ethyl ester 
• 67-56-1 methanol 
• 88050-17-3 N-Fmoc-trans-4-Hydroxy-L-Proline 

Downstream Products

• 122364-65-2 Boc-Tyr-DMet-Gly-Phe-1-2,3,4,6-tetra-O-benzyl-β-glcp> Hyp-OMe 
• 191793-76-7 (S)-4-Fluoro-pyrrolidine-1,2-dicarboxylic acid 1-(9H-fluoren-9-ylmethyl) ester 

Relevant articles and documents

The implications of (2S,4S)-hydroxyproline 4-O-glycosylation for prolyl amide isomerization

The conformations of peptides and proteins are often influenced by glycans O-linked to serine (Ser) or threonine (Thr). (25,4R)-4-Hydroxyproline (Hyp), together with L-proline (Pro), are interesting targets for O-glycosylation because they have a unique influence on peptide and protein conformation. In previous work we found that glycosylation of Hyp does not affect the N-terminal amide transieis ratios (Ktrans/cis) or the rates of amide isomerization in model amides. The stereoisomer of Hyp-(25,4S)-4-hydroxyproline (hyp)-is rarely found in nature, and has a different influence both on the conformation of the pyrrolidine ring and on Ktrans/cis Glycans attached to hyp would be expected to be projected from the opposite face of the prolyl side chain relative to Hyp; the impact this would have on K trans/cis was unknown. Measurements of 3J coupling constants indicate that the glycan has little impact on the Cy-endo conformation produced by hyp. As a result, it was found that the D-galactose residue extending from a Cy-endo pucker affects both K trans/cis and the rate of isomerization, which is not found to occur when it is projected from a Cy-exo pucker; this reflects the different environments delineated by the proline side chain. The enthalpic contributions to the stabilization of the trans amide isomer may be due to disruption of intramolecular interactions present in hyp; the change in enthalpy is balanced by a decrease in entropy incurred upon glycosylation. Because the different stereoisomers-Hyp and hyp-project the O-linked carbohydrates in opposite spatial orientations, these glycosylated amino acids may be useful for understanding of how the projection of a glycan from the peptide or protein backbone exerts its influence.

Me3SI-promoted chemoselective deacetylation: a general and mild protocol

A Me3SI-mediated simple and efficient protocol for the chemoselective deprotection of acetyl groups has been developedviaemploying KMnO4as an additive. This chemoselective deacetylation is amenable to a wide range of substrates, tolerating diverse and sensitive functional groups in carbohydrates, amino acids, natural products, heterocycles, and general scaffolds. The protocol is attractive because it uses an environmentally benign reagent system to perform quantitative and clean transformations under ambient conditions.

A novel somatostatin mimic with broad somatotropin release inhibitory factor receptor binding and superior therapeutic potential

A rational drug design approach, capitalizing on structure-activity relationships and involving transposition of functional groups from somatotropin release inhibitory factor (SRIF) into a reduced size cyclohexapeptide template, has led to the discovery o