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The effect of peptide length on the cleavage kinetics of 2‐chlorotrityl resin‐bound ethers
Author(s) -
Kocsis László,
Ruff Ferenc,
Orosz György
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.745
Subject(s) - chemistry , trifluoroacetic acid , peptide , steric effects , cleavage (geology) , kinetics , hydrolysis , medicinal chemistry , solvent , serine , solvation , organic chemistry , amino acid , peptide synthesis , stereochemistry , biochemistry , enzyme , geotechnical engineering , physics , quantum mechanics , fracture (geology) , engineering
Different characteristics of cleavage kinetics of resin‐bound amino alcohols and their peptide derivatives were observed in acid containing protic and aprotic solvent mixtures. The hydrolysis reactions are hindered by steric crowding around the cleaving CO bond and accelerated by the special solvation effect of CF 3 CH 2 OH on the peptide chain as well as the increase of the strength and concentration of the acid. In trifluoroacetic acid containing mixtures, trifluoroacetylation of the peptide alcohols was detected. The appearance of O ‐trifluoroacetyl serine and threonine derivatives is detected in cleavage mixtures containing trifluoroacetic acid in anhydrous solvent. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.