Side-chain control of β-peptide secondary structures

Design principles

Research output: Contribution to journalArticle

143 Citations (Scopus)

Abstract

As one of the most important families of non-natural polymers with the propensity to form well-defined secondary structures, the β-peptides are attracting increasing attention. The compounds incorporating β-amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of β-peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side-chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the β-peptide foldamers. The folding propensity is influenced by local torsional, side-chain to backbone and long-range side-chain interactions. Although β-peptide foldamers are sensitive to solvent, the systematic choice of the side-chain pattern and spatiality allows the design of the desired specific secondary structure. The application of β-peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions.

Original languageEnglish
Pages (from-to)3657-3666
Number of pages10
JournalEuropean Journal of Biochemistry
Volume270
Issue number18
DOIs
Publication statusPublished - Sep 2003

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Peptides
Biochemistry
Pharmaceutical Chemistry
Conformations
Polymers
Amino Acids

Keywords

  • β-amino acids
  • β-peptides
  • Conformational control
  • Foldamers
  • Non-natural polymers
  • Stereochemistry

ASJC Scopus subject areas

  • Biochemistry

Cite this

Side-chain control of β-peptide secondary structures : Design principles. / Martinek, T.; Fülöp, F.

In: European Journal of Biochemistry, Vol. 270, No. 18, 09.2003, p. 3657-3666.

Research output: Contribution to journalArticle

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