Molecular and Structural Biology Division, Central Drug Research Institute, CSIR, Lucknow, 226001, India.
Amino Acids. 2011 Feb;40(2):749-59. doi: 10.1007/s00726-010-0744-7. Epub 2010 Sep 21.
Membrane-interaction and assembly of a leucine zipper peptide (LZP), and its single (SASA) and double (DASA) alanine-substituted analog onto mammalian, hRBCs and 3T3 cells and bacteria, Escherichia coli and Staphylococcus aureus were studied as a model system to understand the plausible role of assembly on their contrasting cytotoxic but similar bactericidal activities. Peptides' ability to depolarize and damage the membrane organization of hRBC and 3T3 cells decreased from LZP to SASA and to DASA which may be related to their decrease in assembly onto these mammalian live cells and oligomerization states in the presence of these cell membranes or zwitterionic PC/Chol lipid vesicles. However, LZP and its analogs showed appreciable similarities in damaging or depolarizing the E. coli or S. aureus cells, which further matched with their comparable assembly and oligomerization either onto these live cells or the cell membranes or in the presence of negatively charged PC/PG lipid vesicles.
作为一个模型系统,研究了亮氨酸拉链肽(LZP)及其单(SASA)和双(DASA)丙氨酸取代类似物与哺乳动物、人红细胞(hRBC)和 3T3 细胞以及细菌大肠杆菌和金黄色葡萄球菌的膜相互作用和组装,以了解组装对它们具有相似杀菌但不同细胞毒性的可能作用。肽使 hRBC 和 3T3 细胞的膜组织去极化和损伤的能力从 LZP 降低到 SASA 再到 DASA,这可能与其在这些哺乳动物活细胞上的组装减少以及在存在这些细胞膜或两性离子 PC/胆固醇脂质体时的寡聚状态有关。然而,LZP 及其类似物在损伤或去极化大肠杆菌或金黄色葡萄球菌细胞方面表现出相当大的相似性,这与它们在这些活细胞或细胞膜上或在带负电的 PC/PG 脂质体存在下的组装和寡聚状态相当匹配。