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

doi:10.1002/cbic.200900175

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 journal › Article › peer-review

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 language	English
Pages (from-to)	1978-1981
Number of pages	4
Journal	ChemBioChem
Volume	10
Issue number	12
DOIs	https://doi.org/10.1002/cbic.200900175
Publication status	Published - Aug 17 2009
Externally published	Yes

Keywords

Liposomes
Peptides
Phospholipids
Structure-property relationships
Vesicles

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

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10.1002/cbic.200900175

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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 journal › Article › peer-review

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