Biochemical and Biophysical Research Communications
Dehydro-enkephalins. IV. Discriminative recognition of delta and mu opiate receptors by enkephalin analogs
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Peptides
Cited by (77)
Differential receptor binding characteristics of consecutive phenylalanines in μ-opioid specific peptide ligand endomorphin-2
2007, Bioorganic and Medicinal ChemistryAn exploratory density functional study on N- and C- protected trans- α,β-didehydroalanine
2000, Journal of Molecular Structure: THEOCHEMCitation Excerpt :They have also been found to play a role in the biosynthesis of certain amino acids including lanthionine [1,14] and d-alanine in lantibiotics [1]. As our scientific knowledge progressed, α,β-dehydroamino acid residues have also started to be used to modify bioactive molecules such as enkephalins [15–17], gramicidin S [18,19] and sarasilin [20]. The importance of α,β-dehydroamino acid residues stems from their special structural and electronic properties.
Prospects in computational Molecular Medicine: A Millennial Mega-project on peptide folding
2000, Journal of Molecular Structure: THEOCHEMCitation Excerpt :The α,β-dehydroamino acid residues occur widely in various classes of natural and synthetic drugs, although they are most commonly found in classes of antibiotics such as “lantibiotics” (lanthionine containing gene-encoded peptides with antibiotic properties such as nisin [47,48], subtilin [47,49] and ancovenin [47]) and the thiopeptide antibiotics [50,51] berninamycin A, B, C and D. They are also increasingly used in the synthesis of enkephalin analogues having different potencies and selectivities from the parent compound [52–54]. The simplest α,β-dehydroamino acid is ΔAla Fig. 30, having no substituents on its beta carbon.
Conformational properties of peptides containing dehydro amino acids
1998, Journal of Molecular Structure: THEOCHEMA convenient cross-coupling route to α,β,γ,δ-unsaturated amino acids
1997, Tetrahedron Letters