An NMR Study on the Phase Change of Lipid Membranes by an Antimicrobial Peptide, Protegrin-1

被引:4
|
作者
Kim, Chul [1 ]
机构
[1] Hannam Univ, Dept Chem, Taejon 305811, South Korea
关键词
Antimicrobial peptide; Protegrin-1; Toroidal pore; (2)H solid-state NMR; Phase change; SOLID-STATE NMR; ACTIVE AUREIN PEPTIDES; FROGS LITORIA-AUREA; BILAYERS; MAGAININ; PORES; ORIENTATION; MODEL; MECHANISMS; RESISTANCE;
D O I
10.5012/bkcs.2010.31.02.372
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Membrane disruption by an antimicrobial peptide, protegrin-1 (PG-1), was investigated by measuring the (2)H solid-state nuclear magnetic resonance (SSNMR) spectra of 1-palmitoyl-d(31)-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC_d31) in the mixture of PG-1 and POPC_d(31) lipids deposited on thin cover-glass plates. The experimental line shapes of anisotropic (2)H SSNMR spectra measured at various peptide-to-lipid (P/L) ratios were simulated reasonably by assuming the mosaic spread of bilayers containing pore structures or the coexistence of the mosaic spread of bilayers and a fast-tumbling isotropic phase. Within a few days of incubation in the hydration chamber, the pores were formed by the peptide in the POPC_d(31) and POPC_d(31)/cholesterol membranes. However, the formation of the pores was not clear in the POPC_d(31)/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol (POPG) membrane. Over a hundred days after hydration, a rapidly rotating isotropic phase increased in the POPC_d(31) and the POPC_d(31)/cholesterol membranes with the higher P/L ratios, but no isotropic phase appeared in the POPC_d(31)/POPG membrane. Cholesterol added in the POPC bilayer acted as a stabilizer of the pore structure and suppressed the formation of a fast-tumbling isotropic phase.
引用
收藏
页码:372 / 378
页数:7
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