title: Biological activity of fragments and analogues of the potent dimeric opioid peptide, biphalin.
abstract: The synthesis and biological activity of two fragments of the very potent opioid peptide biphalin, showed that Tyr-D-Ala-Gly-Phe-NH-NH<-Phe is the minimal fragment necessary to express equal affinities and the same biological activity profile as the parent biphalin. The replacement of N'-Phe with other L- or D- lipophilic amino acids showed the possibility of modification of receptor efficacy of the analogues.
authors.affiliation: Department of Chemistry, University of Arizona, Tucson 85721, USA.
authors.forename: A W
authors.initials: AW
authors.lastname: Lipkowski
authors.forename: A
authors.initials: A
authors.lastname: Misicka
authors.forename: P
authors.initials: P
authors.lastname: Davis
authors.forename: D
authors.initials: D
authors.lastname: Stropova
authors.forename: J
authors.initials: J
authors.lastname: Janders
authors.forename: M
authors.initials: M
authors.lastname: Lachwa
authors.forename: F
authors.initials: F
authors.lastname: Porreca
authors.forename: H I
authors.initials: HI
authors.lastname: Yamamura
authors.forename: V J
authors.initials: VJ
authors.lastname: Hruby
mesh_terms: D000595:Amino Acid Sequence; D000700:Analgesics / Q000737:chemistry / Q000494:pharmacology*; D004745:Enkephalins / Q000737:chemistry / Q000494:pharmacology*; D017450:Receptors, Opioid, mu / Q000187:drug effects
chemical_list: D000700:Analgesics; D004745:Enkephalins; D017450:Receptors, Opioid, mu; C053673:biphalin