Abstract
Cationic amyloid fibrils, including the Semen Enhancer of Virus Infection (SEVI), have recently been described in human semen. Simple methods for quantitating these fibrils are needed to improve our understanding of their biological function. We performed high-throughput screening to identify molecules that bind SEVI, and identified a small molecule (8E2), that fluoresced brightly in the presence of SEVI and other cationic fibrils. 8E2 bound SEVI with almost 40-fold greater affinity than thioflavin-T, and could efficiently detect high molecular weight fibrils in human seminal fluid.
Original language | English (US) |
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Pages (from-to) | 5199-5202 |
Number of pages | 4 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 23 |
Issue number | 18 |
DOIs | |
State | Published - Sep 15 2013 |
Bibliographical note
Funding Information:Supported by NIH grants T32AI049815 (DE), R21AI094511 . This publication was also supported in part by the University of Rochester Center for AIDS Research (NIH P30AI078498 ) and by a Drug Development pilot award from the University of Rochester School of Medicine & Dentistry .
Keywords
- Amyloid
- Fluorescence
- SEVI
- Semen
- Thioflavin T