Synthesis and biological actions of highly potent and prolonged acting biotin-labeled melanotropins.
Chaturvedi. D N DN; Knittel. J J JJ; Hruby. V J VJ; Castrucci. A M AM; Hadley. M E ME
Key Findings
- Biotin‑linked melanotan‑I analogues keep the same potency as the original peptide
- They show prolonged activity in frog and lizard skin bioassays
- The biotinylated peptides are resistant to inactivation by alpha‑chymotrypsin
Practical Outcomes
- The study suggests that biotin‑tagging could make melanotan‑I last longer and be more stable, hinting at future longer‑acting formulations. However, these compounds are still experimental and not ready for personal use, so no dosing changes are recommended now.
Summary
Scientists attached a biotin tag to a super‑potent version of the tanning peptide melanotan‑I and found it works just as well as the original but stays active longer in lab skin tests and resists enzyme breakdown.
Abstract
Biocytin derivatives of a superpotent analogue of alpha-melanotropin, [Nle4,D-Phe7]-alpha-MSH, were prepared. [N alpha-Bct-Ser1, Nle4,D-Phe7]-alpha-MSH and [12-Bct-N alpha-dodecanoyl-Ser1,Nle4,D-Phe 7]- alpha-MSH were synthesized by solid-phase techniques, and the coupling of biotin and 12-aminododecanoic acid was achieved through their succinimido esters. These melanotropins possessed almost identical actions to [Nle4,D-Phe 7]- alpha-MSH as determined by several melanocyte bioassays. Both biocytin derivatives were highly potent agonists and exhibited prolonged biological activity as determined in the frog and lizard skin bioassays. Both biotinylated peptides were at least equipotent to alpha-MSH in stimulating Cloudman S91 mouse melanoma tyrosinase activity. The analogues were resistant to inactivation by alpha-chymotrypsin.
Study Information
pubmed
1984
10.1021/jm00377a005