The influence of the terminal amino acids of alpha-MSH on its biological action in B16 murine melanoma cells has been systematically studied. Fragments of alpha-MSH lacking various sequences of terminal residues were synthesized by solid-phase peptide synthesis and their binding affinity to melanoma cells was measured using a radioreceptor assay. Biological activity was determined by measuring both tyrosinase activity and melanogenesis. The relative affinities and activities of the fragments generally followed the same pattern as found previously in other assay systems (frog and lizard bioassay and Cloudman S91 mouse melanoma), with the three amino acids at each terminal not being essential for binding and biological activity, although the C-terminal amino acids 11-13 are more important than those in the N-terminus. The differences in biological activity between the fragments can be explained by their relative binding affinities for the receptor.
|Number of pages||6|
|Publication status||Published - 1994|
- Amino Acid Sequence Amino Acids/*chemistry Animals Binding, Competitive/physiology Melanins/analysis Melanoma, Experimental/*metabolism Mice Molecular Sequence Data Monophenol Monooxygenase/analysis Radioligand Assay Receptors, Pituitary Hormone/*metabolism Structure-Activity Relationship Tumor Cells, Cultured alpha-MSH/*chemistry/metabolism/physiology