Comparative Bioinformatics Analysis of the Alpha-Crystallin Gene Family in Homo sapiens and Danio rerio: From Gene Structure to 3D Modeling

Alpha-Crystallin proteins are essential molecular chaperones that maintain eye lenstransparency and prevent cataract formation. This study presents a comparative in silicoanalysis of the Alpha-Crystallin gene family in Homo sapiens and Danio rerio to elucidateevolutionary divergence following teleost-specific whole-genome duplication. We analyzedorthologous CRYAA and CRYAB genes alongside zebrafish paralogs using a comprehensivebioinformatic pipeline including ExPASy ProtParam, GSDS 2.0, MEGA12, MEME Suite,and AlphaFold. Results indicate that while the core Alpha-Crystallin Domain (ACD) retainsa highly conserved beta-sandwich fold, significant divergence occurs in terminal regions.Notably, the zebrafish cryabb paralog exhibits a distinct basic isoelectric point (pI 9.39),contrasting with the acidic nature of other family members, which suggests potentialneofunctionalization within the aquatic lens environment. Furthermore, promoter analysisreveals a regulatory shift from stress-response prioritization (HSF1) in humans todevelopmental control (Sox2 and Pax6) in zebrafish. These findings provide criticalmolecular insights into how duplicated genes diverge to fulfill distinct physiological roleswhile preserving essential chaperone functions