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báo cáo hóa học:" Peptide inhibitors of dengue virus and West Nile virus infectivity"

Tuyển tập các báo cáo nghiên cứu về hóa học được đăng trên tạp chí sinh học đề tài : Peptide inhibitors of dengue virus and West Nile virus infectivity | Virology Journal BioMed Central Research Open Access Peptide inhibitors of dengue virus and West Nile virus infectivity Yancey M Hrobowski1 Robert F Garry1 2 and Scott F Michael 3 Address Department of Microbiology and Immunology Tulane University Health Sciences Center New Orleans Louisiana 70112 USA 2Graduate Program in Cellular and Molecular Biology Tulane University New Orleans LA 70112 USA and 3Biotechnology Program Florida Gulf Coast University Fort Myers FL 33965 USA Email Yancey M Hrobowski - yhrobows@tulane.edu Robert F Garry - rfgarry@tulane.edu Scott F Michael - smichael@fgcu.edu Corresponding author Published 01 June 2005 Received 20 May 2005 Virology Journal 2005 2 49 doi 10.1186 1743-422X-2-49 Accepted 0I June 2005 This article is available from http www.virologyj.cOm content 2 1 49 2005 Hrobowski et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Viral fusion proteins mediate cell entry by undergoing a series of conformational changes that result in virion-target cell membrane fusion. Class I viral fusion proteins such as those encoded by influenza virus and human immunodeficiency virus HIV contain two prominent alpha helices. Peptides that mimic portions of these alpha helices inhibit structural rearrangements of the fusion proteins and prevent viral infection. The envelope glycoprotein E of flaviviruses such as West Nile virus WNV and dengue virus DENV are class II viral fusion proteins comprised predominantly of beta sheets. We used a physio-chemical algorithm the Wimley-White interfacial hydrophobicity scale WWIHS 1 in combination with known structural data to identify potential peptide inhibitors of WNV and DENV infectivity that target the viral E protein. Viral inhibition assays confirm that