The mechanism of self-association of human ▫$\gamma$▫-D crystallin from molecular dynamics simulations
ID Brudar, Sandi (Author), ID Hribar-Lee, Barbara (Author)

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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:γ-D crystallin, self-assembly, arginine, MD simulation
Work type:Article
Typology:1.01 - Original Scientific Article
Organization:FKKT - Faculty of Chemistry and Chemical Technology
Publication status:Published
Publication version:Version of Record
Number of pages:8 str.
Numbering:Vol. 386, art. 122461
PID:20.500.12556/RUL-148272 This link opens in a new window
ISSN on article:0167-7322
DOI:10.1016/j.molliq.2023.122461 This link opens in a new window
COBISS.SI-ID:157958915 This link opens in a new window
Publication date in RUL:09.08.2023
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Record is a part of a journal

Title:Journal of molecular liquids
Shortened title:J. mol. liq.
COBISS.SI-ID:15382277 This link opens in a new window


License:CC BY-NC 4.0, Creative Commons Attribution-NonCommercial 4.0 International
Description:A creative commons license that bans commercial use, but the users don’t have to license their derivative works on the same terms.

Secondary language

Keywords:gama-D-kristalin, samozdruževanje, arginin, simulacija molekulske dinamike


Funder:NIH - National Institutes of Health
Project number:RM1GM135136

Funder:ARRS - Slovenian Research Agency
Project number:BI-US/22-24-125

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