Jonathon R. Sawyer
Jonathon R. Sawyer has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
- Allison Ackerman
Resolute Bio, 48 Dunham Rd., Suite 5400, Beverly, MA 01915, USA
1 shared publication - Brad L. Pentelute
Resolute Bio, 48 Dunham Rd., Suite 5400, Beverly, MA 01915, USA
1 shared publication - David J. Diller
Data2Discovery Consulting, East Windsor, New Jersey 08520, United States
1 shared publication - Gianpaolo Gobbo
XtalPi Inc., 245 Main Street, Cambridge, Massachusetts 02142, United States
1 shared publication - Jon Swanson
Eudoxia Life Sciences, 520 Squire Hill Rd., Cheshire, CT 06410, USA
1 shared publication - Joseph A. Audie
Eudoxia Life Sciences, 520 Squire Hill Rd., Cheshire, CT 06410, USA
1 shared publication
Latest Publications
- Open Access
Design, Structure–Activity Relationships, and Computational Modeling Studies of a Series of α-Helix Biased, Ultra-Short Glucagon-like Peptide-1 Receptor Agonists
A systematic structure–activity and computational modeling analysis of a series of glucagon-like peptide-1 receptor (GLP-1R) agonists based upon an ultra-short GLP-1 peptide, H-His-Aib-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Bip-Bip-NH2, was conducted. This highly potent 11-mer peptide led to a deeper understanding of the α-helical bias of strategic α-methylation within the linear parent template as well as optimization of GLP-1R agonist potency by 1000-fold. These data were correlated with previously reported co-structures of both full-length GLP-1 analogs and progenitor N-terminal GLP-1 fragment analogs related to such ultra-short GLP-1R agonist peptides. Furthermore, the development of a quantitative structure–activity relationship (QSAR) model to analyze these findings is described in this study.
Open AccessDesign, Structure–Activity Relationships, and Computational Modeling Studies of a Series of α-Helix Biased, Ultra-Short Glucagon-like Peptide-1 Receptor Agonists
A systematic structure–activity and computational modeling analysis of a series of glucagon-like peptide-1 receptor (GLP-1R) agonists based upon an ultra-short GLP-1 peptide, H-His-Aib-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Bip-Bip-NH2, was conducted. This highly potent 11-mer peptide led to a deeper understanding of the α-helical bias of strategic α-methylation within the linear parent template as well as optimization of GLP-1R agonist potency by 1000-fold. These data were correlated with previously reported co-structures of both full-length GLP-1 analogs and progenitor N-terminal GLP-1 fragment analogs related to such ultra-short GLP-1R agonist peptides. Furthermore, the development of a quantitative structure–activity relationship (QSAR) model to analyze these findings is described in this study.