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

A J Souers; A Rosenquist; E M Jarvie; M Ladlow; W Feniuk; J A Ellman

doi:10.1016/s0960-894x(00)00552-7

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

Bioorg Med Chem Lett. 2000 Dec 18;10(24):2731-3. doi: 10.1016/s0960-894x(00)00552-7.

Authors

A J Souers¹, A Rosenquist, E M Jarvie, M Ladlow, W Feniuk, J A Ellman

Affiliation

¹ Department of Chemistry, University of California, Berkeley 94720, USA.

PMID: 11133079
DOI: 10.1016/s0960-894x(00)00552-7

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Binding, Competitive
Humans
Inhibitory Concentration 50
Ligands
Molecular Mimicry*
Receptors, Somatostatin / antagonists & inhibitors
Somatostatin / analogs & derivatives*
Somatostatin / chemical synthesis
Somatostatin / metabolism
Structure-Activity Relationship

Substances

Ligands
Receptors, Somatostatin
Somatostatin

Grants and funding

GM-53696/GM/NIGMS NIH HHS/United States