Cataract, the major cause of blindness worldwide occurs due to the misfolding and aggregation of the protein crystallin, which constitute a major portion of the lens protein. Other than the whole protein crystallin, the peptide sequences generated from crystallin as a result of covalent protein damage have also been shown to possess and foster protein aggregation, which can be established as crystallin aggregation models. Thus, the disaggregation or inhibition of these protein aggregates could be a viable approach to combat cataract and preserve lens proteostasis. Herein, we tried to explore the disruption as well as inhibition of the intact α-crystallin protein and α-crystallin derived model peptide aggregates by l-3,4-dihydroxyphenylalanine (levodopa) coated gold (Au) nano/micro-roses as modulators. Thioflavin T fluorescence enhancement assay, and electron microscopic analysis were being employed to probe the anti-aggregation behavior of the Au nano/micro-roses towards the aggregating α-crystallin peptides/protein. Further, computational studies were performed to reveal the nature of molecular interactions between the levodopa molecule and the α-crystallin derived model peptides. Interestingly, both levodopa coated Au nano/micro-roses were found to be capable of inhibiting as well as preventing the aggregation of the intact α-crystallin protein and other model peptides derived from it.

白内障是世界范围内失明的主要原因，这是由于蛋白质晶体蛋白的错误折叠和聚集所致，而晶体蛋白构成了晶状体蛋白质的主要部分。除了整个蛋白结晶蛋白外，由于共价蛋白损伤而从结晶蛋白产生的肽序列也已显示出具有并促进蛋白质聚集，可以将其建立为结晶蛋白聚集模型。因此，这些蛋白质聚集体的分解或抑制可能是对抗白内障和保留晶状体蛋白稳态的可行方法。在本文中，我们试图探索的破坏以及抑制完整α晶状体蛋白和α-晶状的衍生通过模型肽聚集升-3,4-二羟基苯丙氨酸（左旋多巴）包被的金（Au）纳米/微玫瑰作为调节剂。硫黄素T荧光增强测定法和电子显微镜分析被用来探测金纳米/微玫瑰对聚集的α-晶状蛋白肽/蛋白质的抗聚集行为。此外，进行了计算研究以揭示左旋多巴分子与α-晶体蛋白衍生的模型肽之间的分子相互作用的性质。有趣的是，发现左旋多巴涂覆的两种金纳米/微玫瑰都能够抑制以及防止完整的α-晶状体蛋白和其他衍生自其的模型肽的聚集。