Aggregation of resin-bound peptides during solid-phase peptide synthesis. Prediction of difficult sequences

V. Krchnak, Z. Flegelova, Josef Vagner

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Nonrandom incomplete aminoacylation of a pendent peptide chain on an insoluble polymeric support during solid-phase peptide synthesis is sequence-dependent and is caused by aggregation of peptide chains, manifested by a decreased swelling capacity. The volume of the swollen peptidyl-resin after each coupling during the syntheses of 87 sequence unrelated peptides was measured, and for each amino acid and aggregation parameter, <Pa>, was derived that reflects the propensity of the swollen volume of peptidyl-resin to decrease during peptide synthesis. These aggregation parameters were used to predict potentially difficult sequences.

Original languageEnglish (US)
Pages (from-to)450-454
Number of pages5
JournalInternational Journal of Peptide and Protein Research
Volume42
Issue number5
StatePublished - 1993
Externally publishedYes

Fingerprint

Solid-Phase Synthesis Techniques
Agglomeration
Resins
Peptides
Aminoacylation
Swelling
Amino Acids

Keywords

  • β-sheet
  • Aggregation parameter
  • Continuous-flow solid-phase peptide synthesis
  • Difficult sequence
  • Multiple synthesis
  • Prediction of difficult coupling

ASJC Scopus subject areas

  • Biochemistry

Cite this

Aggregation of resin-bound peptides during solid-phase peptide synthesis. Prediction of difficult sequences. / Krchnak, V.; Flegelova, Z.; Vagner, Josef.

In: International Journal of Peptide and Protein Research, Vol. 42, No. 5, 1993, p. 450-454.

Research output: Contribution to journalArticle

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