Peptide triazole inactivators of HIV-1: how do they work and what is their potential?
2015; Future Science Ltd; Volume: 7; Issue: 17 Linguagem: Inglês
10.4155/fmc.15.152
ISSN1756-8927
AutoresIrwin Chaiken, Adel A. Rashad,
Tópico(s)Click Chemistry and Applications
ResumoFuture Medicinal ChemistryVol. 7, No. 17 CommentaryPeptide triazole inactivators of HIV-1: how do they work and what is their potential?Irwin Chaiken & Adel A RashadIrwin Chaiken*Author for correspondence: E-mail Address: irwin.chaiken@drexelmed.edu Department of Biochemistry & Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USA & Adel A Rashad Department of Biochemistry & Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USAPublished Online:24 Nov 2015https://doi.org/10.4155/fmc.15.152AboutSectionsView ArticleView Full TextPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareShare onFacebookTwitterLinkedInReddit View articleKeywords: AIDScell entryenvelope protein antagonismHIV-1infection inhibitionmacrocyclepeptidomimeticsvirus inactivationReferences1 Acharya P, Lusvarghi S, Bewley CA, Kwong PD. HIV-1 gp120 as a therapeutic target: navigating a moving labyrinth. Expert Opin. Ther. Targets 19(6), 765–783 (2015).Crossref, Medline, CAS, Google Scholar2 Swindells S, Flexner C, Fletcher CV, Jacobson JM. The critical need for alternative antiretroviral formulations, and obstacles to their development. J. Infect. Dis. 204(5), 669–674 (2011).Crossref, Medline, Google Scholar3 Wyatt R, Kwong PD, Desjardins E et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393(6686), 705–711 (1998).Crossref, Medline, CAS, Google Scholar4 Jiao J, Rebane AA, Ma L, Gao Y, Zhang Y. Kinetically coupled folding of a single HIV-1 glycoprotein 41 complex in viral membrane fusion and inhibition. Proc. Natl Acad. Sci. USA 112(22), E2855–E2864 (2015).Crossref, Medline, CAS, Google Scholar5 Doms RW. Beyond receptor expression: the influence of receptor conformation, density, and affinity in HIV-1 infection. Virology 276(2), 229–237 (2000).Crossref, Medline, CAS, Google Scholar6 Do Kwon Y, Pancera M, Acharya P et al. Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env. Nat. Struct. Mol. Biol. 22(7), 522–531 (2015).Crossref, Medline, CAS, Google Scholar7 Julien JP, Cupo A, Sok D et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342(6165), 1477–1483 (2013).Crossref, Medline, CAS, Google Scholar8 Munro JB, Gorman J, Ma X et al. Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Science 346(6210), 759–763 (2014).Crossref, Medline, CAS, Google Scholar9 Bastian AR, Contarino M, Bailey LD et al. Interactions of peptide triazole thiols with Env gp120 induce irreversible breakdown and inactivation of HIV-1 virions. Retrovirology 10, 153 (2013).Crossref, Medline, Google Scholar10 Bastian AR, Kantharaju, McFadden K et al. Cell-Free HIV-1 virucidal action by modified peptide triazole inhibitors of Env gp120. ChemMedChem 6(8), 1335–1339 (2011).Crossref, Medline, CAS, Google Scholar11 Contarino M, Bastian AR, Kalyana Sundaram RV et al. Chimeric cyanovirin-MPER recombinantly engineered proteins cause cell-free virolysis of HIV-1. Antimicrob. Agents Chemother. 57(10), 4743–4750 (2013).Crossref, Medline, CAS, Google Scholar12 Bastian AR, Nangarlia A, Bailey LD et al. Mechanism of multivalent nanoparticle encounter with HIV-1 for potency enhancement of peptide triazole virus inactivation. J. Biol. Chem. 290(1), 529–543 (2015).Crossref, Medline, CAS, Google Scholar13 Biorn AC, Cocklin S, Madani N et al. Mode of action for linear peptide inhibitors of HIV-1 gp120 interactions. Biochemistry 43(7), 1928–1938 (2004).Crossref, Medline, CAS, Google Scholar14 Ferrer M, Harrison SC. Peptide ligands to human immunodeficiency virus type 1 gp120 identified from phage display libraries. J. Virol. 73(7), 5795–5802 (1999).Crossref, Medline, CAS, Google Scholar15 Gopi HN, Tirupula KC, Baxter S, Ajith S, Chaiken IM. Click chemistry on azidoproline: high-affinity dual antagonist for HIV-1 envelope glycoprotein gp120. ChemMedChem 1(1), 54–57 (2006).Crossref, Medline, CAS, Google Scholar16 Rostovtsev VV, Green LG, Fokin VV, Sharpless KB. A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed. Engl. 41(14), 2596–2599 (2002).Crossref, Medline, CAS, Google Scholar17 Gopi H, Cocklin S, Pirrone V et al. Introducing metallocene into a triazole peptide conjugate reduces its off-rate and enhances its affinity and antiviral potency for HIV-1 gp120. J. Mol. Recognit. 22(2), 169–174 (2009).Crossref, Medline, CAS, Google Scholar18 Gopi H, Umashankara M, Pirrone V et al. Structural determinants for affinity enhancement of a dual antagonist peptide entry inhibitor of human immunodeficiency virus type-1. J. Med. Chem. 51(9), 2638–2647 (2008).Crossref, Medline, CAS, Google Scholar19 Cocklin S, Gopi H, Baxter S, Chaiken I. A dual action peptide GP120 inhibitor that is effective against multiple HIV-1 clades. FASEB J. 20(4), A465–A465 (2006).Crossref, Google Scholar20 McFadden K, Fletcher P, Rossi F et al. Antiviral breadth and combination potential of peptide triazole HIV-1 entry inhibitors. Antimicrob. Agents Chemother. 56(2), 1073–1080 (2012).Crossref, Medline, CAS, Google Scholar21 Umashankara M, McFadden K, Zentner I et al. The active core in a triazole peptide dual-site antagonist of HIV-1 gp120. ChemMedChem 5(11), 1871–1879 (2010).Crossref, Medline, CAS, Google Scholar22 Bailey LB, Kalyana Sundram RV, Li H et al. Disulfide sensitivity in the Env protein underlies lytic inactivation of HIV-1 by peptide triazole thiols. ACS Chem. Biol. doi:10.1021/acschembio.5b00381 (2015).Crossref, Medline, Google Scholar23 Emileh A, Tuzer F, Yeh H et al. A model of peptide triazole entry inhibitor binding to HIV-1 gp120 and the mechanism of bridging sheet disruption. Biochemistry 52(13), 2245–2261 (2013).Crossref, Medline, CAS, Google Scholar24 Aneja R, Rashad AA, Li H et al. Peptide triazole inactivators of HIV-1 utilize a conserved two-cavity binding site at the junction of the inner and outer domains of Env gp120. J. Med. Chem. 58(9), 3843–3858 (2015).Crossref, Medline, CAS, Google Scholar25 Rashad AA, Kalyana Sundaram RV, Aneja R, Duffy C, Chaiken I. Macrocyclic envelope glycoprotein antagonists that irreversibly inactivate HIV-1 before host cell encounter. J. Med. Chem. 58(18), 7603–7608 (2015).Crossref, Medline, CAS, Google Scholar26 Rashad AA, Kalyana Sundaram RV, Nangarlia A, Aneja R, Duffy C, Chaiken I. Macrocyclic HIV-1 envelope glycoprotein antagonists. Presented at: Structural Biology Related to HIV/AIDS. Natcher Conference Center, Bethesda, Maryland, USA, 18–19 June 2015.Google Scholar27 Bastian AR. Irreversible breakdown of HIV-1 by peptide triazole thiols and multivalent gold nanoparticle conjugates [PhD thesis]. Ann Arbor, Drexel University, MI, USA (2014).Google ScholarFiguresReferencesRelatedDetailsCited ByAltered Env conformational dynamics as a mechanism of resistance to peptide-triazole HIV-1 inactivators9 October 2021 | Retrovirology, Vol. 18, No. 1Therapeutic potential of HIV-1 entry inhibitor peptidomimetics17 February 2021 | Experimental Biology and Medicine, Vol. 246, No. 9Protein- and Peptide-Based Virus Inactivators: Inactivating Viruses Before Their Entry Into Cells25 May 2020 | Frontiers in Microbiology, Vol. 11Recognition of HIV-inactivating peptide triazoles by the recombinant soluble Env trimer, BG505 SOSIP.66411 March 2017 | Proteins: Structure, Function, and Bioinformatics, Vol. 85, No. 5Targeting cell surface HIV-1 Env protein to suppress infectious virus formationVirus Research, Vol. 235Chemical optimization of macrocyclic HIV-1 inactivators for improving potency and increasing the structural diversity at the triazole ring1 January 2017 | Organic & Biomolecular Chemistry, Vol. 15, No. 37Pyrazolo[1,5-a]pyrimidine-based macrocycles as novel HIV-1 inhibitors: a patent evaluation of WO201512318219 July 2016 | Expert Opinion on Therapeutic Patents, Vol. 26, No. 9 Vol. 7, No. 17 Follow us on social media for the latest updates Metrics Downloaded 55 times History Published online 24 November 2015 Published in print November 2015 Information© Future science LtdKeywordsAIDScell entryenvelope protein antagonismHIV-1infection inhibitionmacrocyclepeptidomimeticsvirus inactivationFinancial & competing interests disclosurePeptide triazole studies have been supported by National Institutes of General Medical Sciences and Allergy and Infectious Diseases, NIH; National Science Foundation; United States Agency for international Development; WW Smith Charitable Trust; Schlumberger Foundation; and Drexel University. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.No writing assistance was utilized in the production of this manuscript.PDF download
Referência(s)