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Molecular dynamic study of the antimicrobial peptide maculatin 1.1 stabilization of the preformed pore (CROSBI ID 643364)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa

Sonavane, Yogesh ; Zoranić, Larisa Molecular dynamic study of the antimicrobial peptide maculatin 1.1 stabilization of the preformed pore // International workshop on Biomembranes: The consequences of complexity.. 2016

Podaci o odgovornosti

Sonavane, Yogesh ; Zoranić, Larisa

engleski

Molecular dynamic study of the antimicrobial peptide maculatin 1.1 stabilization of the preformed pore

Antimicrobial peptides (AMP) are the first line of defense against pathogens in all organisms [1]. The mechanism by which these peptides break structure can be by tearing up the lipid bilayer or by inducing the pore formation in the membrane [2, 3]. The key element of the AMPs activity is that they are highly selective, being toxic against a broad range of microorganisms, and not to the host cells. The part of the extensive study which exploits the high level of detail obtainable via molecular dynamics simulations of AMP maculatin in membrane environment, is presented in the following study. We analyzed stabilization of the preformed pore in the neutral phosphatidylcholine (PC) membranes with the different chain length. Our aim is to understand possible relation between lipid composition and some of the proposed mechanisms of action of the antimicrobial peptides.

antimicrobial peptides; molecular dynamics; maculatin; membranes

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Podaci o prilogu

2016.

objavljeno

Podaci o matičnoj publikaciji

International workshop on Biomembranes: The consequences of complexity.

Podaci o skupu

International workshop on Biomembranes: The consequences of complexity

poster

16.09.2016-19.09.2016

Espoo, Finska

Povezanost rada

Fizika

Poveznice