共 33 条
[1]
Henderson J.M., Waring A.J., Separovic F., Lee K.Y.C., Antimicrobial peptides share a common interaction driven by membrane line tension reduction, Biophys. J., 111, pp. 2176-2189, (2016)
[2]
Panteleev P.V., Bolosov I.A., Balandin S.V., Ovchinnikova T.V., Structure and biological functions of ß-hairpin antimicrobial peptides, Acta Naturae., 7, pp. 37-47, (2015)
[3]
Shenkarev Z.O., Balandin S.V., Trunov K.I., Paramonov A.S., Sukhanov S.V., Barsukov L.I., Arseniev A.S., Ovchinnikova T.V., Molecular mechanism of action of ß-hairpin antimicrobial peptide arenicin: oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers, Biochemistry., 50, pp. 6255-6265, (2011)
[4]
Fuertes G., Gimenez D., Esteban-Martin S., Sanchez-Munoz O.L., Salgado J., A lipocentric view of peptide-induced pores, Eur. Biophys. J., 40, pp. 399-415, (2011)
[5]
Perrin B.S., Fu R., Cotten M.L., Pastor R.W., Simulations of membrane-disrupting peptides II: AMP piscidin 1 favors surface defects over pores, Biophys. J., 111, pp. 1258-1266, (2016)
[6]
Kabelka I., Vacha R., Optimal conditions for opening of membrane pore by amphiphilic peptides, J. Chem. Phys., 143, (2015)
[7]
Pan J., Tieleman D.P., Nagle J.F., Kucerka N., Tristram-Nagle S., Alamethicin in lipid bilayers: Combined use of X-ray scattering and MD simulations, Biochim. Biophys. Acta Biomembr., 1788, pp. 1387-1397, (2009)
[8]
Qian S., Wang W., Yang L., Huang H.W., Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores, Proc. Natl. Acad. Sci. USA., 105, pp. 17379-17383, (2008)
[9]
He K., Ludtke S., Heller W., Huang H., Mechanism of alamethicin insertion into lipid bilayers, Biophys. J., 71, pp. 2669-2679, (1996)
[10]
Lee M.-T., Hung W.-C., Chen F.-Y., Huang H.W., Many-body effect of antimicrobial peptides: On the correlation between lipid’s spontaneous curvature and pore formation, Biophys. J., 89, pp. 4006-4016, (2005)