MT-1 10mg

About This Compound

MT-1 is the D-phenylalanine-substituted analog [Nle4, D-Phe7]-α-MSH (referenced in the literature interchangeably as NDP-MSH), a modification of the endogenous tridecapeptide α-MSH designed for enzymatic resistance. Receptor mutagenesis research has mapped how this D-isomer engages alternate contact points on the melanocortin-1 receptor compared with the natural L-isomer hormone. The way a left-handed and a right-handed glove fit the same hand through different construction, the D-isomer and L-isomer ligands are studied for reaching the same receptor pocket by way of distinct molecular contacts.

Research Context

Frändberg, Muceniece, Prusis, Wikberg, and Chhajlani (Biochemical and Biophysical Research Communications, 1994; PMID 8060302) used site-directed mutagenesis of the melanocortin-1 receptor to show that the D-isomer [Nle4, D-Phe7]-α-MSH retains binding affinity at receptor mutants that sharply reduce affinity for the natural L-isomer hormone, providing early evidence of stereoselective binding epitopes on a G-protein-coupled receptor. Yang, Dickinson, Haskell-Luevano, and Gantz (Journal of Biological Chemistry, 1997; PMID 9287296) examined site-directed mutagenesis of acidic and aromatic melanocortin-1 receptor residues to identify contact points shared across this analog and related melanocortin peptides. Frändberg, Doufexis, Kapas, and Chhajlani (Biochemical and Biophysical Research Communications, 2001; PMID 11237737) studied the role of cysteine residues in melanocortin-1 receptor structure, reporting that a single point mutation converted the analog from a receptor agonist to an antagonist in cell-based cAMP signaling assays.

Research Use Disclaimer

For Research Use Only. Not for human consumption.