کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1357925 | 981304 | 2014 | 11 صفحه PDF | دانلود رایگان |

Structure–activity relationship studies of the cyclopentapeptide CXCR4 antagonists (cyclo(-l-/d-Arg1-Arg2-2-Nal3-Gly4-d-Tyr5-)) suggest that the l-/d-Arg1-Arg2-2-Nal3 tripeptide sequence contained within these cyclopentapeptides serves as a recognition motif for peptidic CXCR4 antagonists. Starting by dissecting the cyclopentapeptide structure and reintroducing cyclic constraints in a stepwise manner, we here report a novel class of scaffold-based tripeptidomimetic CXCR4 antagonists based on the d-Arg-Arg-2-Nal motif. Biological testing of the prototype compounds showed that they represent new peptidomimetic hits; importantly, the modular nature of the scaffold provides an interesting starting point for future ligand optimization.
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Journal: Bioorganic & Medicinal Chemistry - Volume 22, Issue 17, 1 September 2014, Pages 4759–4769