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
Biochemistryjournal_title
Biochemistryauthors
Massotte D,Dasseux JL,Sauve P,Cyrklaff M,Leonard K,Pattus Fdoi
10.1021/bi00445a029subject
Has Abstractpub_date
1989-09-19 00:00:00pages
7713-9issue
19eissn
0006-2960issn
1520-4995journal_volume
28pub_type
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