Core chemotype diversification in the HIV-1 entry inhibitor class using field-based bioisosteric replacement
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چکیده
منابع مشابه
The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core.
The three-dimensional structure of the complex between an HIV-1 cell-entry inhibitor selected from screening a combinatorial library of non-natural building blocks and the central, trimeric, coiled-coil core of HIV-1 gp41 has been determined by X-ray crystallography. The biased combinatorial library was designed to identify ligands binding in nonpolar pockets on the surface of the coiled-coil c...
متن کاملRoot , Protein Design of an HIV - 1 Entry Inhibitor
www.sciencemag.org (this information is current as of August 6, 2008 ): The following resources related to this article are available online at http://www.sciencemag.org/cgi/content/full/291/5505/884 version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/cgi/content/full/291/5505/884#otherarticles , 1...
متن کاملA novel small-molecule inhibitor of HIV-1 entry
BACKGROUND Antiretroviral therapy has transformed HIV-1 infection into a managed condition with near-normal life expectancy. However, a significant number of patients remain with limited therapeutic options due to HIV-1 resistance, side effects, or drug costs. Further, it is likely that current drugs will not retain efficacy, due to risks of side effects and transmitted resistance. RESULTS We...
متن کاملProtein design of an HIV-1 entry inhibitor.
Human immunodeficiency virus type-1 (HIV-1) membrane fusion is promoted by the formation of a trimer-of-hairpins structure that brings the amino- and carboxyl-terminal regions of the gp41 envelope glycoprotein ectodomain into close proximity. Peptides derived from the carboxyl-terminal region (called C-peptides) potently inhibit HIV-1 entry by binding to the gp41 amino-terminal region. To test ...
متن کاملGrifonin-1: A Small HIV-1 Entry Inhibitor Derived from the Algal Lectin, Griffithsin
BACKGROUND Griffithsin, a 121-residue protein isolated from a red algal Griffithsia sp., binds high mannose N-linked glycans of virus surface glycoproteins with extremely high affinity, a property that allows it to prevent the entry of primary isolates and laboratory strains of T- and M-tropic HIV-1. We used the sequence of a portion of griffithsin's sequence as a design template to create smal...
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ژورنال
عنوان ژورنال: Bioorganic & Medicinal Chemistry Letters
سال: 2016
ISSN: 0960-894X
DOI: 10.1016/j.bmcl.2015.10.080