The Influence of the Mixed DPC:SDS Micelle on the Structure and Oligomerization Process of the Human Cystatin C.

摘要: Human cystatin C (hCC), a member of the superfamily papain-like cysteine protease inhibitors, is most widespread in human body fluids. Physiologically active hCC monomer, which dimerization and oligomerization lead to formation inactive, insoluble amyloid form protein, strictly associated with cerebral angiopathy, severe state causing death among young patients. It known, that biological membranes may accelerate processes amyloidogenic proteins. Therefore, this study, we describe an influence membrane mimetic environment-mixed dodecylphosphocholine:sodium dodecyl sulfate (DPC:SDS) micelle (molar ratio 5:1)-on effect oligomerization. The hCC-micelle interactions were analyzed size exclusion chromatography, circular dichroism, nuclear magnetic resonance spectroscopy. experiments performed on wild-type (WT) C, two variants-V57P V57G. Collected experimental data supplemented molecular dynamic simulations, making it possible highlight binding interface select residues involved micelle. Obtained shows mixed DPC:SDS does not protein even reverses process.