The structural and functional consequences of melatonin and serotonin on human ?B-crystallin and their dual role in the eye lens transparency.

Crystallins are the major soluble lens proteins, and ?-crystallin, the most important protective protein of the eye lens, has two subunits (?A and ?B) with chaperone activity. ?B-crystallin (?B-Cry) with a relatively wide tissue distribution has an innate ability to interact effectively with the misfolded proteins, preventing their aggregation. Melatonin ...
and serotonin have also been identified in relatively high concentrations in the lenticular tissues. This study investigated the effect of these naturally occurring compounds and medications on the structure, oligomerization, aggregation, and chaperone-like activity of human ?B-Cry. Various spectroscopic methods, dynamic light scattering (DLS), differential scanning calorimetry (DSC), and molecular docking have been used for this purpose. Based on our results, melatonin indicates an inhibitory effect on the aggregation of human ?B-Cry without altering its chaperone-like activity. However, serotonin decreases ?B-Cry oligomeric size distribution by creating hydrogen bonds, decreases its chaperone-like activity, and at high concentrations increases protein aggregation.
Mesh Terms:
Crystallins, Humans, Lens, Crystalline, Melatonin, Molecular Chaperones, Molecular Docking Simulation, Serotonin
Biochim Biophys Acta Proteins Proteom
Date: Sep. 01, 2023
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