Synthesis and properties of equine beta-melanotropin analogs with substitution in residue position 1.
Abstract: Five analogs of equine β-melanotropin have been synthesized by the solid phase method. The NH2-terminal aspartic acid was substituted with amino acids (Gly, Trp, Ile, Lys and Nα-acetyl-Asp) differing widely in physicochemical properties. On the basis of their lipolytic potencies it was concluded that this position plays a negligible role in this activity.
Publication Date: 1983-04-01 PubMed ID: 6862766DOI: 10.1111/j.1399-3011.1983.tb03116.xGoogle Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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This research sought to synthesize and study the properties of five variants of equine β-melanotropin, by substituting the amino acid at the first residue position, to understand its impact on lipolytic activities. The researchers concluded that changes at this position have insignificant effects on these activities.
Research Method
- The research was conducted by synthesizing five analogs of equine β-melanotropin, a peptide hormone known for its role in skin pigmentation and lipolysis. This was done through a solid phase method, a process in which the peptide is bound to a solid support, allowing for efficient and flexible synthesis.
- The specific method employed involved replacing the amino acid aspartic acid at the first residue position with other amino acids: Glycine (Gly), Tryptophan (Trp), Isoleucine (Ile), Lysine (Lys), and Nα-acetyl-Aspartic acid (Nα-acetyl-Asp). These amino acids were selected due to their diverse physicochemical properties, allowing the researchers to observe potential differences in reaction and response.
Finding and Conclusion
- The impact of the substitutions on lipolytic activity was assessed. Lipolysis is the process of breaking down lipids, commonly known as fats in the body. This is a fundamental biological process linked with metabolism and energy regulation.
- Contrary to expectations, the variations at the NH2-terminal position, being varied with different amino acids, did not significantly influence the lipolytic activity of the peptides. This suggests that the aspartic acid residue in the first position of the β-melanotropin sequence has a negligible effect on the hormone’s lipolytic potencies.
Implication
- This finding has implications for our understanding of peptide hormones, such as β-melanotropin, and how alterations in their sequence affect functionality. Specifically, it sheds light on how changes to the first residue position have limited to no effects on their lipid breakdown capacity.
- This is important in hormone research, where understanding the characteristics of these complex molecules and how peptide sequencing influences their function is key. This discovery could potentially influence future research and synthesis of hormones and their analogues.
Cite This Article
APA
Nádasdi L, Yamashiro D, Li CH, Izdebski J.
(1983).
Synthesis and properties of equine beta-melanotropin analogs with substitution in residue position 1.
Int J Pept Protein Res, 21(4), 364-368.
https://doi.org/10.1111/j.1399-3011.1983.tb03116.x Publication
Researcher Affiliations
MeSH Terms
- Animals
- Horses
- Lipolysis / drug effects
- Melanocyte-Stimulating Hormones / analogs & derivatives
- Melanocyte-Stimulating Hormones / chemical synthesis
- Melanocyte-Stimulating Hormones / pharmacology
- Structure-Activity Relationship
Grant Funding
- GM-2907 / NIGMS NIH HHS
Citations
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