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Chem Pharm Bull (Tokyo) ; 70(4): 293-299, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35370207

RESUMO

We designed and synthesized non-peptide organic molecular ligands for integrin αvß3. Candidate ligands featured amidino analog and carboxy groups as binding sites on either side of a spacer, which consisted of benzophenone or an analog, such as diphenyl sulfide, diphenyl sulfoxide, diphenyl sulfone, or diphenyl ether. Competitive binding assays to integrin αvß3 with respect to [125I]echistatin were used to determine inhibitory activity of the synthetic ligands. Ligands bearing 2-aminobenzimidazoyl and glycyl groups separated by a benzophenone spacer demonstrated more potent binding than did a linear Arg-Gly-Asp (RGD) tripeptide that represents the native integrin αvß3 binding motif. Ligands possessing 2-aminobenzimidazoyl and carboxy groups and diphenyl sulfoxide or diphenyl ether spacers inhibited binding of [125I]echistatin with IC50 values similar to that of the linear RGD tripeptide.


Assuntos
Integrina alfaVbeta3 , Sequência de Aminoácidos , Sítios de Ligação , Integrina alfaVbeta3/química , Integrina alfaVbeta3/metabolismo , Ligantes , Peso Molecular
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