Hydrophobic matching between protein and membranes: A case study of α-crystallins

Jui-Kai Chen¹, Jheng-Hao Lin¹, Yu-Ting Liu², Ming-Tao Lee^1,2*

¹Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan
²Department of Physics, National Central University, Taoyuan, Taiwan

* Presenter:Ming-Tao Lee, email:mtlee@nsrrc.org.tw

Hydrophobic matching has been considered as an important mechanism for protein-membrane interaction. Besides theoretical calculations and simulations, rare direct evidence was observed experimentally. Here, DOPC and Di20:1PC were used as model membranes to interact with αA-crystallin and αB-crystallin, which are water-soluble proteins in eye lens. The α-crystallins are able to carry out their chaperone activity to maintain the transparency of eye lens. CD (Circular Dichroism) was used to monitor binding behavior between α-crystallins and lipid vesicles. The water-based method was developed to prepare multilamellar samples of protein-lipid mixture for LXD (Lamellar X-ray Diffraction). The good sample quality makes precise measurements of X-ray diffraction on protein-induced structural changes of membranes feasible. Furthermore, the chaperone activity assays were used to examine anti-aggregation levels of α-crystallins in the absence and presence of lipid membranes. All measurements were conducted in a series o

Keywords: Hydrophobic matching, α-crystallins, membranes, Lamellar X-ray Diffraction (LXD), Circular Dichroism (CD)