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- W2161694092 abstract "Starting with a cyclic peptide of moderate potency as a VLA-4 antagonist, highly potent and conformationally defined cyclic peptides were developed incorporating a constrained tyrosine and an achiral Asp-Pro spacer. N-Acyl phenylalanine derivatives were also discovered to have VLA-4 antagonist activity. During the course of development of this series, we found that the active acylphenylalanines mimic the pharmacophores present in the cyclic peptides and hypothesized that they bind to the same site on VLA-4. This insight guided our optimization strategy. Based on the emerging SAR, as well as insights from the recent X-ray crystal structure of the integrin αvβ3 bound to a RGD containing cyclic peptide, we propose a binding model for these compounds. Keywords: vla-4 antagonists, vascular cell adhesion molecule, asthma, inflammatory bowel disease, vcam/vla-4 interaction, acylphenylalanines, sar" @default.
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- W2161694092 date "2004-10-01" @default.
- W2161694092 modified "2023-09-27" @default.
- W2161694092 title "The Discovery of VLA-4 Antagonists" @default.
- W2161694092 doi "https://doi.org/10.2174/1568026043387502" @default.
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