Binding of Mono, Bi and Tridomain Proteins to Zwitterionic and Anionic Vesicles： Asymmetric Location of Anionic Phospholipids in Mixed Zwitterionic/Anionic Vesicles and Cooperative Binding
Binding of Mono, Bi and Tridomain Proteins to Zwitterionic and Anionic Vesicles： Asymmetric Location of Anionic Phospholipids in Mixed Zwitterionic/Anionic Vesicles and Cooperative Binding作者机构：Institute for Molecular Science University of Valencia Valencia E-46071 Spain Energesis Chair of Interdisciplinary Technology Saint Vincent Martyr Catholic University of Valencia Valencia E-46003 Spain
出 版 物：《Journal of Life Sciences》 (生命科学（英文版）)
年 卷 期：2011年第5卷第3期
页 面：167-181页
学科分类：090502[农学-动物营养与饲料科学] 081702[工学-化学工艺] 08[工学] 0817[工学-化学工程与技术] 0905[农学-畜牧学] 09[农学]
主 题：Protein-lipid interaction sigmoid adsorption isotherm transbilayer asymmetry anionic phospholipid asymmetric location cooperative binding hill plot.
摘 要：Lysozyme, myoglobin and BSA were used as models of globular proteins covering a wide range of pl. The purpose is to extend the studies to anionic lipid bilayers. Electrostatics is studied in cationic protein adsorption to zwitterionic PC and anionic mixed PC/PG SUVs. Protein adsorption is investigated in SUVs along with changes of fluorescence emission spectra. Partition coefficients and cooperativity parameters are calculated. At pl binding obtains maximum while at lower or higher pHs binding decreases. In Gouy-Chapman formalism activity coefficient goes with square charge, which deviations indicate asymmetric location of anionic phospholipid in the inner leaflet, in mixed SUVs for lysozyme- and myoglobin-PC/PG systems, in agreement with experiments and molecular dynamics simulations. Vesicles bind myoglobin anti-cooperatively while lysozyme-BSA cooperativitivey. A model is proposed for both, which composes two protein sub-layers with different structures and properties. Hill coefficient reflects subunit cooperativity of bi and tridomain proteins.
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