The effect of peptide length on the cleavage kinetics of 2-chlorotrityl resin-bound ethers

László Kocsis, Ferenc Ruff, György Orosz

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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 C-O bond and accelerated by the special solvation effect of CF3CH2OH 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.

Original languageEnglish
Pages (from-to)428-436
Number of pages9
JournalJournal of Peptide Science
Volume12
Issue number6
DOIs
Publication statusPublished - Jun 1 2006

Keywords

  • Cleavage
  • Kinetics
  • Peptide alcohol
  • Trifluoroacetylation
  • Trityl resin

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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