Onikanni Sunday Amos, Fadaka Adewale Oluwaseun, Dao Tran Nhat Phong, Munyembaraga Valens, Nyau Vincent, Sibuyi Nicole Remaliah Samantha, Ajayi Morenike Grace, Nhung Nguyen Thi Ai, Ejiofor Emmanuel, Ajiboye Basiru Olaitan, Le Minh Hoang, Chang Hen-Hong
College of Medicine, Graduate Institute of Biomedical Sciences, China Medical University, Taichung, Taiwan.
Department of Chemical Sciences, Biochemistry Unit, Afe-Babalola University, Ado-Ekiti, Nigeria.
Front Chem. 2025 Jan 17;12:1421534. doi: 10.3389/fchem.2024.1421534. eCollection 2024.
Severe protein clumping in the lens can block light and lead to vision issues in cataract patients. Recent studies have linked β-crystallins, which are key proteins in the lens, to the development of cataracts. Specifically, the S175G/H181Q mutation in the βB2-crystallin gene plays a major role in cataract formation.
To understand how this mutation can be activated, we utilized computational methods to predict activators from Phaseolus vulgaris. The Schrödinger platform was employed to screen bioactive compounds and simulate molecular interactions in order to analyze binding and structural changes.
Our results indicated that these phytochemicals are stable near S175G/H181Q.
These findings suggest novel approaches that could potentially be developed into effective anticataract medications through further refinement and additional testing, ultimately resulting in the creation of more potent agents for cataract treatment.
晶状体中严重的蛋白质聚集会阻挡光线,并导致白内障患者出现视力问题。最近的研究已将晶状体中的关键蛋白质β-晶状体蛋白与白内障的发展联系起来。具体而言,βB2-晶状体蛋白基因中的S175G/H181Q突变在白内障形成中起主要作用。
为了解这种突变是如何被激活的,我们利用计算方法从菜豆中预测激活剂。采用薛定谔平台筛选生物活性化合物并模拟分子相互作用,以分析结合和结构变化。
我们的结果表明,这些植物化学物质在S175G/H181Q附近是稳定的。
这些发现提示了一些新方法,通过进一步优化和额外测试,有可能将其开发成有效的抗白内障药物,最终创制出更有效的白内障治疗药物。