The design and synthesis of potent cyclic peptide VCAM-VLA-4 antagonists incorporating an achiral Asp-Pro mimetic

The Asp-Pro sequence of the cyclic peptide Ac-HN-Tyr-Cys*-Asp-Pro-Cys*-OH (1) could be replaced with the achiral dipeptide mimetic 1-(2-aminoethyl)cyclpentylcarboxylic acid with retention of potent inhibition of the VCAM-VLA-4 interaction.

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Bibliographic Details
Published inBioorganic & medicinal chemistry letters Vol. 10; no. 11; pp. 1171 - 1173
Main Authors FOTOUHI, N, JOSHI, P, FRY, D, COOK, C, TILLEY, J. W, KAPLAN, G, HANGLOW, A, ROWAN, K, SCHWINGE, V, WOLITZKY, B
Format Journal Article
LanguageEnglish
Published Oxford Elsevier 05.06.2000
Subjects
Aspartic Acid - chemistry
Biological and medical sciences
Drug Design
Immunomodulators
Integrin alpha4beta1
Integrins - antagonists & inhibitors
Medical sciences
Molecular Mimicry
Peptides, Cyclic - chemical synthesis
Peptides, Cyclic - chemistry
Peptides, Cyclic - pharmacology
Pharmacology. Drug treatments
Proline - chemistry
Receptors, Lymphocyte Homing - antagonists & inhibitors
Vascular Cell Adhesion Molecule-1 - drug effects
Sulfur nitrogen heterocycle
Ring size
Vascular cell adhesion molecule 1
Cyclic peptides
Peptidomimetic compound
Cell adhesion molecule
In vitro
Spiran
Macrocycle
Pseudopeptide
Organic disulfide
Structure activity relation
Sulfur peptide
Dipeptides
Antagonist
Chemical synthesis
Biological receptor
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Summary:The Asp-Pro sequence of the cyclic peptide Ac-HN-Tyr-Cys*-Asp-Pro-Cys*-OH (1) could be replaced with the achiral dipeptide mimetic 1-(2-aminoethyl)cyclpentylcarboxylic acid with retention of potent inhibition of the VCAM-VLA-4 interaction.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0960-894X
1464-3405
DOI:10.1016/s0960-894x(00)00174-8