122350-59-8

Usage

Uses

Used in Organic Synthesis:
N-Fmoc-trans-4-hydroxy-L-proline methyl ester serves as a key building block in organic synthesis, facilitating the creation of complex molecular structures through its reactive functional groups.
Used in Peptide Chemistry:
In peptide chemistry, N-Fmoc-trans-4-hydroxy-L-proline methyl ester is utilized as a component for the synthesis of peptides, providing a protected form of the amino acid proline that can be selectively deprotected and incorporated into peptide sequences.
Used in Drug Discovery and Development:
N-Fmoc-trans-4-hydroxy-L-proline methyl ester is employed in the preparation of peptide libraries, which are crucial for high-throughput screening in drug discovery. Its presence in these libraries aids in the identification of potential therapeutic agents.
Used in the Synthesis of Peptides and Proteins with Proline Residues:
N-Fmoc-trans-4-hydroxy-L-proline methyl ester is particularly useful in synthesizing peptides and proteins that contain proline, due to its ability to protect the N-terminal amino group and facilitate the incorporation of proline into the peptide backbone.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, N-Fmoc-trans-4-hydroxy-L-proline methyl ester is used as a reagent for the synthesis of bioactive peptides and proteins, contributing to the development of new drugs and therapeutic agents.

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

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

Relevant academic research and scientific papers

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.

Stereoselective syntheses of 4-oxa diaminopimelic acid and its protected derivatives via aziridine ring opening

Regio- and stereoselective aziridine ring opening with oxygen nucleophiles derived from serine and threonine provides a route to stereochemically pure 4-oxa-2,6-diaminopimelic acid (oxa-DAP) and its methyl-substituted derivatives. Oxa-DAP is a substrate of DAP epimerase, a key enzyme for biosynthesis of L-lysine and formation of peptidoglycan precursors. Orthogonally protected analogues of lanthionine and/β-methyllanthionine wherein oxygen replaces sulfur were prepared that could be used for solid-supported peptide synthesis to make oxa derivatives of lantibiotics.

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

Fluorinated peptides incorporating a 4-fluoroproline residue as potential inhibitors of HIV protease

N-Fmoc-4-fluoro-L-proline methyl ester was prepared as an attractive synthon for both solid and solution phase peptide synthesis. Its use for the synthesis of Fmoc-Phe-Pro(F)-OMe and Fmoc-Pro(F)-Val-Val-OMe is presented. Direct fluorination with DAST of a