Abstract
The conformations of all stereoisomers of PMRI cyclotetrapeptide mimetics 1-8 are essentially determined by the predisposition of the diamine to stabilize beta-turns. The peptide mimetics can be regarded as 3D scaffolds for designing molecules with a predictable display of the pharmacophores. We used the models for testing novel RGD analogues as alpha(v)beta(3)-integrin receptor antagonists.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Biomimetic Materials / chemistry*
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Biomimetic Materials / pharmacology*
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Cell Adhesion / drug effects
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Cell Line
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Cell Line, Tumor
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Computer Simulation
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Humans
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Imaging, Three-Dimensional / methods*
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Integrin alphaVbeta3 / metabolism
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Conformation
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Peptides, Cyclic / chemistry*
Substances
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Integrin alphaVbeta3
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Peptides, Cyclic