A Potent α/β-Peptide Analogue of GLP-1 with Prolonged Action in Vivo | Zendy

Lisa M. Johnson | Zendy; Stacey Barrick | Zendy; Marlies V. Hager | Zendy; Amanda McFedries | Zendy; Edwin A. Homan | Zendy; Mary E. Rabaglia | Zendy; Mark P. Keller | Zendy; Alan Attie | Zendy; Alan Saghatelian | Zendy; Alessandro Bisello | Zendy; Samuel H. Gellman | Zendy

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A Potent α/β-Peptide Analogue of GLP-1 with Prolonged Action in Vivo

Author(s) -

Lisa M. Johnson,

Stacey Barrick,

Marlies V. Hager,

Amanda McFedries,

Edwin A. Homan,

Mary E. Rabaglia,

Mark P. Keller,

Alan Attie,

Alan Saghatelian,

Alessandro Bisello,

Samuel H. Gellman

Publication year - 2014

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja507168t

Subject(s) - chemistry , in vivo , peptide , agonist , glucagon like peptide 1 receptor , glucagon like peptide 1 , receptor , g protein coupled receptor , in vitro , biochemistry , pharmacology , type 2 diabetes , endocrinology , diabetes mellitus , medicine , microbiology and biotechnology , biology

Glucagon-like peptide-1 (GLP-1) is a natural agonist for GLP-1R, a G protein-coupled receptor (GPCR) on the surface of pancreatic β cells. GLP-1R agoinsts are attractive for treatment of type 2 diabetes, but GLP-1 itself is rapidly degraded by peptidases in vivo. We describe a design strategy for retaining GLP-1-like activity while engendering prolonged activity in vivo, based on strategic replacement of native α residues with conformationally constrained β-amino acid residues. This backbone-modification approach may be useful for developing stabilized analogues of other peptide hormones.

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