Publication: Identification of N-Terminally Diversified GLP-1R Agonists Using Saturation Mutagenesis and Chemical Design
Identification of N-Terminally Diversified GLP-1R Agonists Using Saturation Mutagenesis and Chemical Design
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Longwell, C. K., Hanna, S., Hartrampf, N., Sperberg, R. A. P., Huang, P.-S., Pentelute, B. L., & Cochran, J. R. (2021). Identification of N-Terminally Diversified GLP-1R Agonists Using Saturation Mutagenesis and Chemical Design. ACS Chemical Biology, 16(1), 58–66. https://doi.org/10.1021/acschembio.0c00722
Abstract
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The glucagon-like peptide 1 receptor (GLP-1R) is a class B G-protein coupled receptor (GPCR) and diabetes drug target expressed mainly in pancreatic β-cells that, when activated by its agonist glucagon-like peptide 1 (GLP-1) after a meal, stimulates insulin secretion and β-cell survival and proliferation. The N-terminal region of GLP-1 interacts with membrane-proximal residues of GLP-1R, stabilizing its active conformation to trigger intracellular signaling. The best-studied agonist peptides, GLP-1 and exendin-4, share sequence homolo
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Creators (Authors)
- Longwell, Chelsea K
- Hanna, Stephanie
- Hartrampf, Nina
- Sperberg, R Andres Parra
- Huang, Po-Ssu
- Pentelute, Bradley L
- Cochran, Jennifer R
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U.S. Department of Commerce
Bristol-Myers Squibb
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Longwell, C. K., Hanna, S., Hartrampf, N., Sperberg, R. A. P., Huang, P.-S., Pentelute, B. L., & Cochran, J. R. (2021). Identification of N-Terminally Diversified GLP-1R Agonists Using Saturation Mutagenesis and Chemical Design. ACS Chemical Biology, 16(1), 58–66. https://doi.org/10.1021/acschembio.0c00722
