Hydrophobic Nanoparticles Reduce the β-Sheet Content of SEVI Amyloid Fibrils and Inhibit SEVI-Enhanced HIV Infectivity

Semen-derived enhancer of virus infection (SEVI) fibrils are naturally abundant amyloid aggregates found in semen that facilitate viral attachment and internalization of human immunodeficiency virus (HIV) in cells, thereby increasing the probability of infection. Mature SEVI fibrils are composed of...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 33(2017), 10 vom: 14. März, Seite 2596-2602
1. Verfasser: Sheik, Daniel A (VerfasserIn)
Weitere Verfasser: Chamberlain, Jeffrey M, Brooks, Lauren, Clark, Melissa, Kim, Young Hun, Leriche, Geoffray, Kubiak, Clifford P, Dewhurst, Stephen, Yang, Jerry
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Amyloid
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520 |a Semen-derived enhancer of virus infection (SEVI) fibrils are naturally abundant amyloid aggregates found in semen that facilitate viral attachment and internalization of human immunodeficiency virus (HIV) in cells, thereby increasing the probability of infection. Mature SEVI fibrils are composed of aggregated peptides exhibiting high β-sheet secondary structural characteristics. Herein, we show that polymers containing hydrophobic side chains can interact with SEVI and reduce its β-sheet content by ∼45% compared with the β-sheet content of SEVI in the presence of polymers with hydrophilic side chains, as estimated by polarization modulation-infrared reflectance absorption spectroscopy measurements. A nanoparticle (NP) formulation of this hydrophobic polymer reduced SEVI-mediated HIV infection in TMZ-bl cells by 60% compared with the control treatment. Although these NPs lacked specific amyloid-targeting groups, thus requiring high concentrations to observe biological activity, the use of hydrophobic interactions to alter the secondary structure of amyloids represents a useful approach to neutralizing the SEVI function. These results could, therefore, have general implications in the design of novel materials that can modify the activity of amyloids associated with a variety of other neurological and systemic diseases 
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650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Research Support, Non-U.S. Gov't 
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700 1 |a Chamberlain, Jeffrey M  |e verfasserin  |4 aut 
700 1 |a Brooks, Lauren  |e verfasserin  |4 aut 
700 1 |a Clark, Melissa  |e verfasserin  |4 aut 
700 1 |a Kim, Young Hun  |e verfasserin  |4 aut 
700 1 |a Leriche, Geoffray  |e verfasserin  |4 aut 
700 1 |a Kubiak, Clifford P  |e verfasserin  |4 aut 
700 1 |a Dewhurst, Stephen  |e verfasserin  |4 aut 
700 1 |a Yang, Jerry  |e verfasserin  |4 aut 
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