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Biophysical Journal 73: 2527-2533 (1997)
© 1997 the Biophysical Society

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Penetration of the insect defensin A into phospholipid monolayers and formation of defensin A-lipid complexes.

R Maget-Dana and M Ptak

Centre de Biophysique Moléculaire CNRS, Orléans, France.

ABSTRACT

Defensin A is an inducible cationic protein secreted in the hemolymph of fleshfly Phormia terranovae larvae in response to bacterial or septic injuries. Defensin A is known to permeabilize the bacteria cell membranes by forming voltage-dependent channels. The penetration of this small protein into lipid monolayers was studied as a function of the polar head and acyl chain length of phospholipids. The extent of penetration by defensin A is higher in monolayers made of anionic phospholipids than in monolayers made of zwitterionic phospholipids (phosphatidylcholines), because of electrostatic interactions. From the analysis of the compression isotherm parameters of mixed defensin A/phospholipid monolayers, it appears that defensin A interacts with phospholipid by forming 1:4 complexes. These complexes are not miscible in the lipid phase and induce microheterogeneity in the lipid membrane. These clusters might be related to the ion-channel structures responsible for the biological activity of defensin A.




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