130832-25-6

Basic information

• Product Name: FMOC-LEU-PRO-OH
• Synonyms: FMOC-LEU-PRO-OH;(9H-Fluoren-9-yl)MethOxy]Carbonyl Leu-Pro-OH
• CAS NO: 130832-25-6
• Molecular Formula: C26H30N2O5
• Molecular Weight: 450.53
• Mol File: 130832-25-6.mol
• Article Data: 5

Chemical Properties

• Boiling Point: 684.9±55.0 °C(Predicted)
• Appearance: /
• Density: 1.252±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 3.51±0.20(Predicted)
• CAS DataBase Reference: FMOC-LEU-PRO-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-LEU-PRO-OH(130832-25-6)
• EPA Substance Registry System: FMOC-LEU-PRO-OH(130832-25-6)

Safety Data

• Hazardous Substances Data: 130832-25-6(Hazardous Substances Data)

Upstream product

• 5497-76-7 L-proline tert-butyl ester hydrochloride 
• 35661-60-0 Fmoc-Leu-OH 
• 2812-46-6 proline tert-butyl ester 
• 184589-14-8 Fluorenylmethoxycarbonylleucyl-proline tert-butyl ester 

Downstream Products

• 6403-35-6 (S)-1-((S)-2-Amino-4-methyl-pentanoyl)-pyrrolidine-2-carboxylic acid 
• 4425-82-5 9-methylene-fluorene 

Relevant articles and documents

Efficient synthesis of a fluorescent farnesylated ras peptide

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Synthesis and anticancer activities of proline-containing cyclic peptides and their linear analogs and congeners

A solution phase method was adopted for the synthesis of proline-containing cyclic pentapeptide 2 and total synthesis of naturally occurring cyclic heptapeptide Reniochalistatin B 3. For the synthesis of 3, both divergent and convergent strategies were used to improve the overall yield from 12 to 25%. Different N and C terminal modified linear analogs and congeners of 2 and 3 were synthesized. Both cyclic peptides 2 and 3 and their linear analogs/congeners were evaluated for anti-cancer activity against HeLa cell line, among which pentapeptide 2 h and hexapeptide 3n with N-terminal protected hexafluoroisopropyl carbamates (HFIPC) interestingly showed higher cytotoxicity with an IC50 of 2.73 and 4.3 μM, respectively compared to their Boc-protected analogs 2a (IC50 20 μM) and 3c (IC50 38.51 μM) and cyclic peptides 2 (>100 μM) and 3 (47 μM). These results were further validated by biological experiments such as colony formation and wound healing assays.

Piperidine is preferred to morpholine for Fmoc cleavage in solid phase glycopeptide synthesis as exemplified by preparation of glycopeptides related to HIV gp120 and mucins

Protected derivatives of the Tn antigens [Fmoc-Ser/Thr(Ac3GalNAcα)-OH, compounds 5 and 8] have been prepared by glycosylation of Fmoc-Ser/Thr- OAllyl with 3,4,6-tri-O-acetyl-2-azido-2-deoxy-D-galactopyranosyl chloride (2), followed by conversion of the azido group to an acetamide and deallylation. The derivatives 5 and 8 were used for solid phase synthesis of glycopeptides related to HIV gp120 and mucins. In these syntheses piperidine was found to give efficient Fmoc removal whereas deprotection with morpholine was slow and incomplete for some steps. In contrast to previous concerns β- elimination and epimerization of glycopeptide stereocenters was not encountered when piperidine was used for Fmoc deprotection. However, it was found that for glycopeptides which contained cysteine residues, de-O- acetylation with methanolic ammonia had to be performed before side-chain deprotection and cleavage from the solid phase.