Surface activity of the insect defensin A and its interactions with lipids in mixed monolayers

Defensin A is an inducible antibacterial protein isolated from the larvae of Phormia terranovae which interacts with membrane cells by forming ion-conducting pores. Defensin A adsorbs at the air-water interface from an aqueous solution and is able to spread as a monolayer. The shape of the compressi...

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Bibliographic Details
Published in:Thin solid films 1996-09, Vol.284, p.841-844
Main Authors: Maget-Dana, R., Hetru, Ch, Ptak, Marius
Format: Article
Language:English
Subjects:
Defensin A
Interfaces
Monolayers
Surface activity
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Summary:Defensin A is an inducible antibacterial protein isolated from the larvae of Phormia terranovae which interacts with membrane cells by forming ion-conducting pores. Defensin A adsorbs at the air-water interface from an aqueous solution and is able to spread as a monolayer. The shape of the compression isotherm curves of defensin monolayers is very sensitive to the pH of the subphase. Defensin A penetrates into lecithin monolayers. In mixed monolayers defensin A and lecithin are at least partially miscible. Plots of the mean molecular area as a function of composition show positive deviations from the additivity rule. The conformational state of defensin A at the air-water interface undergoes a change upon interaction with phospholipids.
ISSN:0040-6090
1879-2731
DOI:10.1016/S0040-6090(95)08460-6