ǂThe ǂmechanism of self-association of human [gamma]-D crystallin from molecular dynamics simulations

Sandi Brudar (Author), Barbara Hribar (Author)

Abstract

The aggregation of human $\gamma$-D crystallin is associated with the age-onset cataract formation. Here, we extensively investigated the self-association mechanism of human $\gamma$-D crystallin through molecular dynamics computer simulations. By mutating the protein surface we found that electrostatic interactions between charged amino acids play a crucial role in its self-association. We have confirmed the two-fold role of arginine molecules. If they are located as residues on the protein surface they can initiate protein contacts and contribute to their stickiness with noteworthy hydrophobic interactions through stacking of their methylene groups. But if they are added as free arginine in the protein solution they can also stabilize it, by associating with the protein surface and also with themselves to form effective inter-protein spacers that obstruct protein aggregation.

Keywords

gama-D-kristalin;samozdruževanje;arginin;simulacija molekulske dinamike;gamma-D-crystallin;self-assembly;arginine;MD simulation;

Data

Language:	English
Year of publishing:	2023
Typology:	1.01 - Original Scientific Article
Organization:	UL FKKT - Faculty of Chemistry and Chemical Technology
UDC:	577.322
COBISS:	157958915
ISSN:	0167-7322
Views:	263
Downloads:	25
Average score:	0 (0 votes)
Metadata:

Other data

Secondary language:	Slovenian
Secondary keywords:	gama-D-kristalin;samozdruževanje;arginin;simulacija molekulske dinamike;
Type (COBISS):	Article
Pages:	str. 1-8
Issue:	ǂVol. ǂ386, [article no.] 122461
Chronology:	15 Sep. 2023
DOI:	10.1016/j.molliq.2023.122461
ID:	19766060