Optimization of a somatostatin mimetic via constrained amino acid and backbone incorporation

Constrained analogues 5– 7 of the potent and subtype selective somatostatin mimetic 1 were prepared by incorporating conformational constraints into the nine-membered heterocyclic scaffold. Each constrained peptidomimetic showed an altered activity profile relative to lead compound 1, with compound...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2000-12, Vol.10 (24), p.2731-2733
Main Authors: Souers, Andrew J., Rosenquist, Asa, Jarvie, Emma M., Ladlow, Mark, Feniuk, Wasyl, Ellman, Jonathan A.
Format: Article
Language:English
Subjects:
Binding, Competitive
Biological and medical sciences
Humans
Inhibitory Concentration 50
Ligands
Medical sciences
Molecular Mimicry
Neuropharmacology
Neurotransmitters. Neurotransmission. Receptors
Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems
Pharmacology. Drug treatments
Receptors, Somatostatin - antagonists & inhibitors
Somatostatin - analogs & derivatives
Somatostatin - chemical synthesis
Somatostatin - metabolism
Structure-Activity Relationship
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Summary:Constrained analogues 5– 7 of the potent and subtype selective somatostatin mimetic 1 were prepared by incorporating conformational constraints into the nine-membered heterocyclic scaffold. Each constrained peptidomimetic showed an altered activity profile relative to lead compound 1, with compound 7 exhibiting a 25-fold and 2-fold binding enhancement against somatostatin receptor subtypes sst4 and sst5, respectively.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(00)00552-7