ArticleMolecular vision2018
αA-crystallin-derived minichaperone stabilizes αAG98R-crystallin by affecting its zeta potential.
Article in Molecular vision, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Regulatory role of serine 59 in the oligomeric dynamics and chaperone function of αB-crystallin.Scientific reports · 2025Article
- Promotion of Protein Solubility and Reduction in Stiffness in Human Lenses by Aggrelyte-1: Implications for Reversing Presbyopia.International journal of molecular sciences · 2023Article
- Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Purpose: The G98R mutant of αA-crystallin is associated with the development of presenile cataracts. In vitro, the recombinant mutant protein exhibits altered structural and functional characteristics, along with the propensity to aggregate by itself and precipitate. Previously, we have reported that the N-terminal aspartate substituted form of the antiaggregation peptide, D Methods: Wild-type αA-crystallin (αAWT) and recombinant mutant αAG98R were purified from Results: Binding of the αA-minichaperone to aggregation-prone αAG98R was accompanied by an increase in the ζ potential from -15.19±0.870 mV corresponding to αAG98R alone to -28.64±1.640 mV for the purified complex. Mass spectrometric analysis identified Conclusions: The αA-crystallin-derived minichaperone stabilizes αAG98R by compensating its lost surface charge. Methods for increasing the ζ potential of aggregating proteins can be a potential approach for therapy to protein aggregation diseases.
Indexed as
Identifiers
29706763PMC5906106What OpenQuestion holds
Registered trials
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