The mechanism of the interaction of α-crystallin and UV-damaged βL-crystallin

α-Crystallin maintains the transparency of the lens by preventing the aggregation of damaged proteins. The aim of our work was to study the chaperone-like activity of native α-crystallin in near physiological conditions (temperature, ionic power, pH) using UV-damaged βL-crystallin as the target prot...

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Veröffentlicht in:	International journal of biological macromolecules 2019-11, Vol.140, p.736-748
Hauptverfasser:	Muranov, K.O., Poliansky, N.B., Chebotareva, N.A., Kleimenov, S.Yu, Bugrova, A.E., Indeykina, M.I., Kononikhin, A.S., Nikolaev, E.N., Ostrovsky, M.A.
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Crystallins - metabolism beta-Crystallins - metabolism Lens, Crystalline - metabolism Molecular chaperone Molecular Chaperones - metabolism Protein Aggregates - physiology Temperature Ultraviolet Rays UV-light α-crystallin βL-crystallin
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Beschreibung
Zusammenfassung:	α-Crystallin maintains the transparency of the lens by preventing the aggregation of damaged proteins. The aim of our work was to study the chaperone-like activity of native α-crystallin in near physiological conditions (temperature, ionic power, pH) using UV-damaged βL-crystallin as the target protein. α-Crystallin in concentration depended manner inhibits the aggregation of UV-damaged βL-crystallin. DSC investigation has shown that refolding of denatured UV-damaged βL-crystallin was not observed under incubation with α-crystallin. α-Crystallin and UV-damaged βL-crystallin form dynamic complexes with masses from 75 to several thousand kDa. The content of UV-damaged βL-crystallin in such complexes increases with the mass of the complex. Complexes containing >10% of UV-damaged βL-crystallin are prone to precipitation whereas those containing
ISSN:	0141-8130 1879-0003
DOI:	10.1016/j.ijbiomac.2019.08.178