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GLUE That Sticks to HIV: A Helix‐Grafted GLUE Protein That Selectively Binds the HIV gp41 N‐Terminal Helical Region
Author(s) -
Walker Susanne N.,
Tennyson Rachel L.,
Chapman Alex M.,
Kennan Alan J.,
McNaughton Brian R.
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402531
Subject(s) - gp41 , human immunodeficiency virus (hiv) , glue , helix (gastropod) , terminal (telecommunication) , chemistry , biophysics , stereochemistry , virology , biology , materials science , genetics , antibody , computer science , epitope , composite material , telecommunications , ecology , snail
Methods for the stabilization of well‐defined helical peptide drugs and basic research tools have received considerable attention in the last decade. Here, we report the stable and functional display of an HIV gp41 C‐peptide helix mimic on a G RAM‐ L ike U biquitin‐binding in E AP45 (GLUE) protein. C‐peptide helix‐grafted GLUE selectively binds a mimic of the N‐terminal helical region of gp41, a well‐established HIV drug target, in a complex cellular environment. Additionally, the helix‐grafted GLUE is folded in solution, stable in human serum, and soluble in aqueous solutions, and thus overcomes challenges faced by a multitude of peptide drugs, including those derived from HIV gp41 C‐peptide.