Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.

ABSTRACT:

Background

The objective of this study was to determine whether the cataract-related G18V variant of human γS-crystallin has increased exposure of hydrophobic residues that could explain its aggregation propensity and/or recognition by αB-crystallin.

Methods

We used an ANS fluorescence assay and NMR chemical shift perturbation to experimentally probe exposed hydrophobic surfaces. These results were compared to flexible docking simulations of ANS molecules to the proteins, starting with the solution-state NMR structures of γS-WT and γS-G18V.

Results

γS-G18V exhibits increased ANS fluorescence, suggesting increased exposed hydrophobic surface area. The specific residues involved in ANS binding were mapped by NMR chemical shift perturbation assays, revealing ANS binding

SUBMITTER: Khago D 

PROVIDER: S-EPMC5942885 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature