期刊論文

學年 113
學期 2
出版(發表)日期 2025-07-01
作品名稱 Screening of small molecules with varying inhibitory effects on islet amyloid peptide aggregation using liquid crystal-based sensors
作品名稱(其他語言)
著者 Ting-Hui Li; Jhih-Wei Huang; Chih-Hsin Chen; Ling-Hsien Tu
單位
出版者
著錄名稱、卷期、頁數 Sensors and Actuators B: Chemical 443, p.138240
摘要 Islet amyloid polypeptide (IAPP) is a hormone co-secreted with insulin from pancreatic β-cells. Under pathological conditions, IAPP aggregates into cytotoxic oligomers and insoluble amyloid fibrils, impairing β-cell function and potentially contributing to type 2 diabetes (T2D). Although various methods have been developed to screen amyloid inhibitors, many are time-consuming and require specialized equipment. Here, we present a label-free liquid crystal (LC)-based sensing platform for monitoring IAPP aggregation in aqueous solutions. At the LC/aqueous interface where the LC adopts a homeotropic orientation, the formation of IAPP aggregates disrupts the LC ordering, resulting in a distinct dark-to-bright optical transition at concentrations as low as 250 nM. We showed that this transition resulted from the formation of peptide oligomers. By using this mechanism, the system effectively differentiates small molecules with varying inhibitory effects on IAPP aggregation, offering a clear visual readout of changes in LC alignment. This platform thus provides a straightforward and efficient tool for real-time monitoring of peptide aggregation and high-throughput screening of potential anti-amyloid and anti-oligomerization compounds, ultimately facilitating the development of therapeutic strategies against T2D and other amyloid-related disorders.
關鍵字 Islet amyloid polypeptide; Anti-aggregation drug; Liquid crystal-based sensor
語言 en
ISSN 0925-4005; 1944-8201
期刊性質 國外
收錄於 SCI
產學合作
通訊作者 Chih-Hsin Chen
審稿制度
國別 NLD
公開徵稿
出版型式 ,電子版
相關連結

機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/127906 )