Premium
Convenient synthesis of collagen‐related tripeptides for segment condensation
Author(s) -
Ellison Aubrey J.,
VanVeller Brett,
Raines Ronald T.
Publication year - 2015
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22700
Subject(s) - chemistry , tripeptide , diketopiperazines , peptide synthesis , peptide , condensation , reagent , protecting group , combinatorial chemistry , morpholine , solid phase synthesis , condensation reaction , organic chemistry , extraction (chemistry) , chloroformate , chromatography , biochemistry , catalysis , physics , alkyl , thermodynamics
Chromatography is a common step in the solution‐phase synthesis of typical peptides, as well as peptide fragments for subsequent coupling on a solid support. Combining known reagents that form readily separable byproducts is shown to eliminate this step, which wastes time and other resources. Specifically, activating carboxyl groups with isobutyl chloroformate or as pentafluorophenyl esters and using N ‐methyl morpholine as a base enable chromatography‐free synthetic routes in which peptide products are isolated from byproducts by facile evaporation, extraction, and trituration. This methodology was used to access tripeptides related to collagen, such as Fmoc‐Pro‐Pro‐Gly‐OH and Fmoc‐Pro‐Hyp( t Bu)‐Gly‐OH, in a purity suitable for solid‐phase segment condensation to form collagen mimetic peptides. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 674–681, 2015.