In:
Macromolecular Bioscience, Wiley, Vol. 23, No. 5 ( 2023-05)
Kurzfassung:
In the human eye lenses, the crystallin proteins facilitate transparency, light refraction, as well as UV light protection. A deregulated balanced interplay between α ‐, β ‐, and γ ‐crystallin can cause cataract. γ D‐crystallin (h γ D) is involved in the energy dissipation of absorbed UV light by energy transfer between aromatic side chains. Early UV‐B induced damage of h γ D with molecular resolution is studied by solution NMR and fluorescence spectroscopy. h γ D modifications are restricted to Tyr 17 and Tyr 29 in the N‐terminal domain, where a local unfolding of the hydrophobic core is observed. None of the tryptophan residues assisting fluorescence energy transfer is modified and h γ D is remained soluble over month. Investigating isotope‐labeled h γ D surrounded by eye lens extracts from cataract patients reveals very week interactions of solvent‐exposed side chains in the C‐terminal h γ D domain and some remaining photoprotective properties of the extracts. Hereditary E107A h γ D found in the eye lens core of infants developing cataract shows under the here used conditions a thermodynamic stability comparable to the wild type but an increased sensitivity toward UV‐B irradiation.
Materialart:
Online-Ressource
ISSN:
1616-5187
,
1616-5195
DOI:
10.1002/mabi.202200526
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2023
ZDB Id:
2039130-4
SSG:
12
Permalink