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

Autori
Sonavane, Yogesh ; Zoranić, Larisa

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
International workshop on Biomembranes: The consequences of complexity. / - , 2016

Skup
International workshop on Biomembranes: The consequences of complexity

Mjesto i datum
Espoo, Finska, 16.09.2016. - 19.09.2016

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
antimicrobial peptides; molecular dynamics; maculatin; membranes

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Fizika

POVEZANOST RADA