Interaction of the pore-forming domain of colicin A with phospholipid vesicles.

Abstract:

:The interaction of the 20-kDa pore-forming domain of colicin A with phospholipid vesicles was investigated by gel permeation chromatography, analytical centrifugation, and electron microscopy. Under the experimental conditions of this study, this peptide was found to interact only with vesicles containing negatively charged phospholipids. It forms a well-defined disklike complex with phosphatidylglycerols with a preference for those containing 12-14 atoms of carbon in their fatty acid chain. This complex has a diameter of 120 A and is about one bilayer thick. It contains nine molecules of peptide and is formed both at acidic pH (pH 5.0) and at neutral pH (pH 7.2).

journal_name

Biochemistry

journal_title

Biochemistry

authors

Massotte D,Dasseux JL,Sauve P,Cyrklaff M,Leonard K,Pattus F

doi

10.1021/bi00445a029

subject

Has Abstract

pub_date

1989-09-19 00:00:00

pages

7713-9

issue

19

eissn

0006-2960

issn

1520-4995

journal_volume

28

pub_type

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