Peptides Mimicking the β7/β8 Loop of HIV‑1 Reverse Transcriptase p51 as “Hotspot-Targeted” Dimerization Inhibitors

A conformationally constrained short peptide designed to target a protein–protein interaction hotspot in HIV-1 reverse transcriptase (RT) disrupts p66-p51 interactions and paves the way to the development of novel RT dimerization inhibitors.

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Bibliographic Details
Published in:	ACS medicinal chemistry letters Vol. 11; no. 5; pp. 811 - 817
Main Authors:	Sánchez-Murcia, Pedro A, de Castro, Sonia, García-Aparicio, Carlos, Jiménez, M. Angeles, Corona, Angela, Tramontano, Enzo, Sluis-Cremer, Nicolas, Menéndez-Arias, Luis, Velázquez, Sonsoles, Gago, Federico, Camarasa, María-José
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 14-05-2020
Subjects:	Letter dimerization inhibitors Constrained peptides dimerization hotspot HIV reverse transcriptase
Online Access:	Get full text
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Description
Summary:	A conformationally constrained short peptide designed to target a protein–protein interaction hotspot in HIV-1 reverse transcriptase (RT) disrupts p66-p51 interactions and paves the way to the development of novel RT dimerization inhibitors.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1948-5875 1948-5875
DOI:	10.1021/acsmedchemlett.9b00623