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Conformations of primary amphipathic carrier peptides in membrane mimicking environments.

Abstract：

:Two peptides designed for drug delivery were generated by the combination of a signal peptide with a nuclear localization sequence and are shown to facilitate the cellular internalization of small molecules which are covalently linked to these peptides. In order to understand the mechanism of internalization, the conformations of the peptides were investigated through different approaches both in solution and in membrane-mimicking environments. These peptides are highly versatile and adopt different conformational states depending on their environment. While in a disordered form in water, they adopt an alpha-helical structure in TFE and in the presence of micelles of SDS or DPC. The structured domain encompasses the hydrophobic part of the peptides, whereas the charged C-termini remain unstructured. In contrast, in the presence of lipids and whatever the nature of the phosphate headgroup, the two peptides mainly adopt an antiparallel beta-sheet form and embed in the lipidic cores. This result suggests that the beta-sheet is responsible for the translocation through the cellular membranes but also questions the conformational state of signal peptides when associated to hydrophilic sequences.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Chaloin L,Vidal P,Heitz A,Van Mau N,Méry J,Divita G,Heitz F

doi

10.1021/bi9708491

subject

Has Abstract

pub_date

1997-09-16 00:00:00

pages

11179-87

issue

37

eissn

0006-2960

issn

1520-4995

pii

bi9708491

journal_volume

36

pub_type

杂志文章

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