Foldameric probes for membrane interactions by induced β-sheet folding

Zsófia Hegedüs, Ildikó Makra, Norbert Imre, A. Hetényi, I. Mándity, E. Monostori, T. Martinek

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Design strategies were devised for α/β-peptide foldameric analogues of the antiangiogenic anginex with the goal of mimicking the diverse structural features from the unordered conformation to a folded β-sheet in response to membrane interactions. Structure-activity relationships were investigated in the light of different β-sheet folding levels.

Original languageEnglish
Pages (from-to)1891-1894
Number of pages4
JournalChemical Communications
Volume52
Issue number9
DOIs
Publication statusPublished - Jan 31 2016

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Peptides
Conformations
Membranes

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Ceramics and Composites
  • Electronic, Optical and Magnetic Materials
  • Surfaces, Coatings and Films
  • Materials Chemistry
  • Metals and Alloys

Cite this

Foldameric probes for membrane interactions by induced β-sheet folding. / Hegedüs, Zsófia; Makra, Ildikó; Imre, Norbert; Hetényi, A.; Mándity, I.; Monostori, E.; Martinek, T.

In: Chemical Communications, Vol. 52, No. 9, 31.01.2016, p. 1891-1894.

Research output: Contribution to journalArticle

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