Inversion of the configuration of a single stereocenter in a β-heptapeptide leads to drastic changes in its interaction with phospholipid bilayers

Toshinori Shimanouchi, Peter Walde, James Gardiner, Stefania Capone, Dieter Seebach, Ryochi Kuboi

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

In summary, a change in the configuration of a single amino acid in a β3-heptapeptide can lead to remarkable changes in the physicochemical properties of the peptide with respect to the interaction with a (protein-free) biomimetic environment. Thus, the presence of an unnatural amino acid configuration in a peptide can have consequences not only with respect to specific interactions with proteins, but also, indirectly, with respect to the interaction with membrane lipids.

Original languageEnglish
Pages (from-to)1978-1981
Number of pages4
JournalChemBioChem
Volume10
Issue number12
DOIs
Publication statusPublished - Aug 17 2009
Externally publishedYes

Fingerprint

Phospholipids
Amino Acids
Biomimetics
Peptides
Membrane Lipids
Proteins

Keywords

  • Liposomes
  • Peptides
  • Phospholipids
  • Structure-property relationships
  • Vesicles

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology

Cite this

Inversion of the configuration of a single stereocenter in a β-heptapeptide leads to drastic changes in its interaction with phospholipid bilayers. / Shimanouchi, Toshinori; Walde, Peter; Gardiner, James; Capone, Stefania; Seebach, Dieter; Kuboi, Ryochi.

In: ChemBioChem, Vol. 10, No. 12, 17.08.2009, p. 1978-1981.

Research output: Contribution to journalArticle

Shimanouchi, Toshinori ; Walde, Peter ; Gardiner, James ; Capone, Stefania ; Seebach, Dieter ; Kuboi, Ryochi. / Inversion of the configuration of a single stereocenter in a β-heptapeptide leads to drastic changes in its interaction with phospholipid bilayers. In: ChemBioChem. 2009 ; Vol. 10, No. 12. pp. 1978-1981.
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