Lactoferrin-Derived Antimicrobial Peptide Induces a Micellar Cubic Phase in a Model Membrane System

• Type: Article in International Scientific Journal
• Date: 2011

Authors

Margarida Bastos (Author) FCUP; Tania Silva (Author) Other; Vitor Teixeira (Author) Other; Kamran Nazmi (Author) Other; Jan G M Bolscher (Author) Other; Sergio S Funari (Author) Other; Daniela Uhrikova (Author) Other

Journal

Title: Biophysical Journal

Vol. 101

Pages: L20-L22

ISSN: 0006-3495

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 22 Citations

Scopus - 25 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-002-NT7

DOI: 10.1016/j.bpj.2011.06.038

Abstract (EN): The observation of a micellar cubic phase is reported for a mixture of an antimicrobial peptide from the Lactoferrin family, LFampin 265-284, and a model membrane system of dimyristoylphosphatidylcholine/dimyristoylphosphatidylglycerol (3:1), as derived from small-angle x-ray diffraction (SAXD) measurements. The system shows remarkable thermotropic polymorphism: the peptide disrupts the lipid bilayer, forming a cubic phase of the space group Pm 3n (t < 28 degrees C), and as the temperature increases it shows a complex phase behavior (not fully clarified by SAXD). The onset, volume fraction of each phase, and phase parameters are seen to vary with peptide/lipid ratio and temperature. The obtained SAXD data represent the first experimental evidence, to our knowledge, of a micellar cubic phase in the context of antimicrobial peptide/membrane interaction. We propose that the micellization of the membrane according to the carpet model, for long proposed as a possible mechanism of action, can go through the formation of a cubic micellar phase.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 3