Influence of alpha-MSH terminal amino acids on binding affinity and biological activity in melanoma cells

U. G. Sahm, G. W. Olivier, S. K. Branch, S. H. Moss, C. W. Pouton

Research output: Contribution to journalArticleResearchpeer-review

Abstract

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.
Original languageEnglish
Pages (from-to)441-446
Number of pages6
JournalPeptides
Volume15
Publication statusPublished - 1994

Keywords

  • 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

Cite this

Sahm, U. G. ; Olivier, G. W. ; Branch, S. K. ; Moss, S. H. ; Pouton, C. W. / Influence of alpha-MSH terminal amino acids on binding affinity and biological activity in melanoma cells. In: Peptides. 1994 ; Vol. 15. pp. 441-446.
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title = "Influence of alpha-MSH terminal amino acids on binding affinity and biological activity in melanoma cells",
abstract = "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.",
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Influence of alpha-MSH terminal amino acids on binding affinity and biological activity in melanoma cells. / Sahm, U. G.; Olivier, G. W.; Branch, S. K.; Moss, S. H.; Pouton, C. W.

In: Peptides, Vol. 15, 1994, p. 441-446.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Influence of alpha-MSH terminal amino acids on binding affinity and biological activity in melanoma cells

AU - Sahm, U. G.

AU - Olivier, G. W.

AU - Branch, S. K.

AU - Moss, S. H.

AU - Pouton, C. W.

N1 - M1 - 3 Sahm, U G Olivier, G W Branch, S K Moss, S H Pouton, C W eng Research Support, Non-U.S. Gov't 1994/01/01 Peptides. 1994;15(3):441-6.

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

KW - 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

M3 - Article

VL - 15

SP - 441

EP - 446

JO - Peptides

JF - Peptides

SN - 0196-9781

ER -