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Article

H101G Mutation in Rat Lens αB-Crystallin Alters Chaperone Activity and Divalent Metal Ion Binding.

Current pharmaceutical biotechnology - 1 Jan 2022

Wu Yi-Ying, Desu Naveen Kumar Reddy, Lu Shou-Yun, Yu Bi-Yu, Kumar Ramya, Huang Fu-Yung

Abstract excerpt

BACKGROUND: The molecular chaperone function of αB-crystallins is heavily involved in maintaining lens transparency and the development of cataracts. OBJECTIVES: The aim of the study was to investigate whether divalent metal ion binding improves the stability and αB-crystallin chaperone activity. METHODS: In this study, we have developed an H101G αB-crystallin mutant and compared the surface hydrophobicity,...

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PMID: 34225616
DOI: 10.2174/1389201022666210702130843

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