| Texto completo | |
| Autor(es): |
Carrer, Manuel
;
Nielsen, Josefine Eilso
;
Cezar, Henrique Musseli
;
Lund, Reidar
;
Cascella, Michele
;
Soares, Thereza A.
Número total de Autores: 6
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Journal of Physical Chemistry Letters; v. 14, n. 31, p. 6-pg., 2023-07-31. |
| Resumo | |
We report a physicochemical investigation of the lipidtransportproperties of model lipid membranes in the presence of the antimicrobialpeptide indolicidin through comparisons of experimental SANS/SAXSscattering techniques to fully atomistic molecular dynamics simulations.In agreement with the experiment, we show that upon peripheral bindingof the peptides, even at low concentrations, lipid flip-flop dynamicsis greatly accelerated. Computer modeling elucidates the interplaybetween structural changes and lipid dynamics induced by peptidesand proposes a mechanism for the mode of action of antimicrobial peptides,assessing the major role of entropy for the catalysis of the flippingevents. The mechanism introduced here is universal for all peptideswith preferential peripheral binding to the membrane as it does notdepend on the specific amino acid sequence. (AU) | |
| Processo FAPESP: | 21/04283-3 - Uma abordagem de múltipla resolução para o polimorfismo de agregados lipopolissacarídicos induzido por metais |
| Beneficiário: | Thereza Amélia Soares da Silva |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |