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Brian C. Wilkes

Researcher at University of Arizona

Publications -  64
Citations -  1914

Brian C. Wilkes is an academic researcher from University of Arizona. The author has contributed to research in topics: Opioid peptide & Agonist. The author has an hindex of 24, co-authored 64 publications receiving 1888 citations. Previous affiliations of Brian C. Wilkes include University of São Paulo.

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alpha-Melanotropin: the minimal active sequence in the frog skin bioassay.

TL;DR: The minimal sequence required for biological activity of alpha-MSH was determined in the frog (Rana pipiens) skin bioassay and a series of fragment analogues were prepared in an attempt to determine the contribution of each individual amino acid to the Biological activity of the native hormone.
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An all D-amino acid opioid peptide with central analgesic activity from a combinatorial library

TL;DR: Simulations using molecular dynamics showed that three amino acid moieties have the same spatial orientation as the corresponding pharmacophoric groups of the opioid peptide PLO17, demonstrating that this peptide may cross the blood-brain barrier.
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TIPP[psi]: a highly potent and stable pseudopeptide delta opioid receptor antagonist with extraordinary delta selectivity.

TL;DR: The more potent compound, TIPP [psi], displayed subnanomolar delta receptor affinity and in direct comparisons with other selective delta ligands was shown to have unprecedented delta specificity.
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α-melanotropin: The minimal active sequence in the lizard skin bioassay

TL;DR: The minimal message sequence for equipotency to alpha-MSH appears to be Ac-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-NH2, since the analog, Ac-[Nle4]-alpha- MSH4-11- NH2, was as active as the native hormone.
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The TIPP opioid peptide family: development of delta antagonists, delta agonists, and mixed mu agonist/delta antagonists.

TL;DR: A definitive model of the receptor-bound conformation of H-Tyr-Tic-(Phe-Phe)-OH-related delta opioid antagonists, which is characterized by all-trans peptide bonds is led to.