由于多位点结合，蛋白质吸附后脂质有序相的重排。
Rearrangement of lipid ordered phases upon protein adsorption due to multiple site binding.
作者信息
Yim H, Kent M S, Sasaki D Y, Polizzotti B D, Kiick K L, Majewski J, Satija S
机构信息
Sandia National Laboratories, Albuquerque, New Mexico, USA.
出版信息
Phys Rev Lett. 2006 May 19;96(19):198101. doi: 10.1103/PhysRevLett.96.198101. Epub 2006 May 16.
Abstract
This study involves the interactions of proteins with Langmuir monolayers of a metal-chelating lipid, where adsorption is driven by a strong specific interaction between histidines on the proteins and divalent metal ions loaded into the lipid headgroups. A comparison of the structural rearrangement of the lipid film upon adsorption of myoglobin and a synthetic peptide, each of which have multiple histidines, with that upon the adsorption of lysozyme, which has only one histidine, suggests that the lipid rearrangement in the former case is due to the multiplicity of binding sites. The kinetics and manner of rearrangement change with the binding energy and film pressure.
摘要
本研究涉及蛋白质与金属螯合脂质的朗缪尔单层之间的相互作用，其中吸附是由蛋白质上的组氨酸与负载在脂质头部基团中的二价金属离子之间的强特异性相互作用驱动的。对肌红蛋白和一种合成肽（两者均具有多个组氨酸）吸附后脂质膜的结构重排与仅具有一个组氨酸的溶菌酶吸附后脂质膜的结构重排进行比较，结果表明前一种情况下的脂质重排是由于结合位点的多样性。重排的动力学和方式随结合能和膜压力而变化。
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