Alpha-defensin dimers adsorb onto microbial membrane anionic phospholipids

Stable Identifier
Reaction [binding]
Homo sapiens
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The alpha-defensin dimers adsorb onto microbial membrane anionic phospholipids, represented here as a complex of alpha-defensin dimers and a representative set of phospholipid molecules 'membrane anionic phospholipids'. The polar topology of defensins, with their spatially separated charged and hydrophobic regions, allows them to insert into microbial cell membranes, which contains more negatively charged phospholipids than mammalian cell membranes (Lohner et al. 1997). Defensins permeabilize membrane vesicles (Lehrer et al. 1989) with a greater effect on vesicles rich in negatively charged phospholipids (Fuji et al. 1993, Wimley et al. 1994).

Literature References
PubMed ID Title Journal Year
2668334 Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity

Daher, KA, Ganz, T, Selsted, ME, Harwig, SS, Barton, A, Lehrer, RI

J Clin Invest 1989
18973303 Mechanisms of alpha-defensin bactericidal action: comparative membrane disruption by Cryptdin-4 and its disulfide-null analogue

Hadjicharalambous, C, Ouellette, AJ, Gizeli, E, Sheynis, T, Shanahan, MT, Jelinek, R

Biochemistry 2008
7833799 Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores

Wimley, WC, White, SH, Selsted, ME

Protein Sci 1994
Orthologous Events
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