Characterization of the Interaction of Human γS Crystallin with Metal Ions and Its Effect on Protein Aggregation.

ABSTRACT: Cataracts are diseases characterized by the opacity of the ocular lens and the subsequent deterioration of vision. Metal ions are one of the factors that have been reported to induce crystallin aggregation. For HγS crystallin, several equivalent ratios of Cu(II) promote protein aggregation. However, reports on zinc are contradictory. To characterize the process of metal ion binding and subsequent HγS crystallin aggregation, we performed dynamic light scattering, turbidimetry, isothermal titration calorimetry, fluorescence, and nuclear magnetic resonance experiments. The data show that both metal ions have multiple binding sites and promote aggregation. Zinc interacts mainly with the N-terminal domain, inducing small conformational changes, while copper interacts with both domains and induc

SUBMITTER: Cardenas R 

PROVIDER: S-EPMC11674332 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature