Institute of Experimental Physics, Faculty of Physics, University of Warsaw, Pasteura 5, 02-093 Warsaw, Poland.
Center of Cellular Immunotherapies, Warsaw University of Life Sciences, 02-786 Warsaw, Poland.
J Phys Chem Lett. 2024 Sep 19;15(37):9543-9547. doi: 10.1021/acs.jpclett.4c01709. Epub 2024 Sep 12.
This study investigates the lasing effects in a Fabry-Perot cavity to discern the binding interactions of thioflavin T (ThT) with various peptides associated with Alzheimer's disease, including Aβ(1-42), KLVFFA, and diphenylalanine (FF) in the condensed phase. Utilizing kinetic lasing measurements, the research explores ThT emission enhancements due to specific groove binding in β-sheet structures and highlights additional contributions from weak surface interactions and solvent-solute interactions. Lasing spectroscopy reveals a lack of transition of the FF system from its native state to an amyloid-like structure, challenging traditional ThT assay interpretations. These findings show the potential of lasing spectroscopy in elucidating the molecular basis of amyloid fibril formation and the development of diagnostic tools for amyloidogenic diseases.
本研究通过法布里-珀罗腔中的激光效应来研究与阿尔茨海默病相关的各种肽（包括 Aβ（1-42）、KLVFFA 和二苯丙氨酸（FF））的硫黄素 T（ThT）结合相互作用。利用动力学激光测量，研究了由于 β-折叠结构中的特定沟槽结合而导致的 ThT 发射增强，并强调了来自弱表面相互作用和溶剂-溶质相互作用的附加贡献。激光光谱学揭示了 FF 体系从其天然状态到类似淀粉样结构的转变缺乏，这对传统的 ThT 分析方法的解释提出了挑战。这些发现表明激光光谱学在阐明淀粉样纤维形成的分子基础以及开发淀粉样变性疾病的诊断工具方面具有潜力。
