The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Peptide lipidation stabilizes structure to enhance biological function
Open accessAbstract
Medicines that decrease body weight and restore nutrient tolerance could improve human diabetes and obesity treatment outcomes. We developed lipid-acylated glucagon analogs that are co-agonists for the glucagon and glucagon-like peptide 1 receptors, and stimulate weight loss and plasma glucose lowering in pre-diabetic obese mice. Our studies identified lipid acylation (lipidation) can increase and balance in vitro potencies of select glucagon analogs for the two aforementioned receptors in a lipidation site-dependent manner. A general capacity for lipidation to enhance the secondary structure of glucagon analogs was recognized, and the energetics of this effect quantified. The molecular structure of a lipid-acylated glucagon analog in water was also characterized. These results support that lipidation can modify biological activity through thermodynamically-favorable intramolecular interactions which stabilize structure. This establishes use of lipidation to achieve specific pharmacology and implicates similar endogenous post-translational modifications as physiological tools capable of refining biological action in means previously underappreciated.
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“Importantly, this demonstrates that the chemical nature of the acylation influences not only the pharmacokinetics of the peptide but also the pharmacophore itself, which further highlights that such modifications are not inert bystanders with respect to biological activity [48] and biodistribution [49].”
From Next generation GLP-1/GIP/glucagon triple agonists normalize body weight in obese mice (2022) · cites this paper as [48]
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Synthesis of Peptide Analogs From Fish Venom With Potential Antimicrobial and Anticancer Activity
de la Salud‐Bea, R., Shen, Q., Frawley, E. R., Brint, A. A., Jenkins, S. V., Dings, R. P. M., Alli, C., & Abhieyighan, P. (2026) · Chemical Biology & Drug Design · doi:10.1111/cbdd.70351
BindingDB Entry 50046601: Small cyclic agonists of iron regulatory hormone hepcidin.
BindingDB (2016) · UC San Diego · doi:10.7270/q2cr5w6z
BindingDB (2020) · UC San Diego · doi:10.7270/q2fn18tn
Metadata
- Authors
- Ward, B. P., Ottaway, N. L., Perez-Tilve, D., Ma, D., Gelfanov, V. M., Tschöp, M. H., & DiMarchi, R. D.
- Affiliations
- Indiana University Bloomington (US)
- University of Cincinnati (US)
- Helmholtz Munich (DE)
- Corresponding author
- Ward, Brian P.
- Venue
- Molecular Metabolism
- Publisher
- Elsevier BV
- Published
- 2013-11
- Volume
- 2
- Issue
- 4
- Pages
- 468-479
- ISSN
- 2212-8778 (ISSN-L)
- PMC
- PMC3854995
- OpenAlex
- W2047944726
- Cited by
- 101
- References
- 43
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 7 · 2023: 5 · 2022: 12 · 2021: 10 · 2020: 9 · 2019: 10 · 2018: 10 · 2017: 9 · 2016: 8 · 2015: 6 · 2014: 4
- FWCI
- 4.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Metabolism (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Site cant be reached (submittedVersion, cc-by-nc-nd)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- glucagon receptor, GLP-1 receptor, weight loss, blood glucose reduction, obesity, diabetes mellitus, prediabetes, intramolecular interactions, post-translational modification, structure-activity relationship
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