Abstract
The endogenous hemorphins are bioactive peptides with activity on opioid receptors. They are extensively studied and summarized in numerous reviews. During the last decade, several research teams have synthesized, characterized, and pharmacologically evaluated synthetic hemorphin analogs containing unusual amino acids, D-amino acids, α-aminophosphonic acids, and their derivatives. The present review summarizes the current studies on short-chain synthetic hemorphin peptide derivates containing non-natural amino acids. This review focuses on the structure–activity relationship analysis, details on specific methods for their characterization, and the advantage of synthetic hemorphin analogs compared to endogenous peptides as potent biologically active compounds with a complex mechanism of action.
Funder
Ministry of Education and Science
Subject
Drug Discovery,Pharmaceutical Science,Molecular Medicine
Reference88 articles.
1. Mielczarek, P., Hartman, K., Drabik, A., Hung, H.-Y., Huang, E.Y.-K., Gibula-Tarlowska, E., Kotlinska, J.H., and Silberring, J. (2021). Hemorphins—From Discovery to Functions and Pharmacology. Molecules, 26.
2. Isolation from bovine brain of a novel analgesic pentapeptide, neo-kyotorphin, containing the Tyr-Arg (kyotorphin)unit;Fukui;Neuropharmacology,1983
3. Hemoglobin research and the origins of molecular medicine;Schechter;Blood J. Am. Soc. Hematol.,2008
4. Hemoglobin induction in mouse macrophages;Liu;Proc. Natl. Acad. Sci. USA,1999
5. Hemoglobin is expressed by alveolar epithelial cells;Newton;J. Biol. Chem.,2006
Cited by
4 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献