P1,P3 Truncated Analogs of Oscillarin and their Inhibitory Activity against Blood Coagulation Factors | Zendy

Stephen Hanessiana | Zendy; Sébastien Guillemette | Zendy; Karolina Ersmark | Zendy

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P1,P3 Truncated Analogs of Oscillarin and their Inhibitory Activity against Blood Coagulation Factors

Author(s) -

Stephen Hanessiana,

Sébastien Guillemette,

Karolina Ersmark

Publication year - 2007

Publication title -

chimia international journal for chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.387

H-Index - 55

eISSN - 2673-2424

pISSN - 0009-4293

DOI - 10.2533/chimia.2007.361

Subject(s) - amide , chemistry , stereochemistry , thrombin , coagulation , phenylalanine , glycine , enzyme , carboxamide , protein subunit , trypsin , amino acid , biochemistry , platelet , biology , medicine , psychiatry , gene , immunology

Based on modeling and available X-ray co-crystal structure data of oscillarin with the enzyme thrombin, a series of P1,P3 truncated analogs were prepared using the azabicyclic octahydroindole carboxamide core as a scaffold. The P1 subunit of the original natural product was replaced by a 4-amidinobenzamide group, and the P3 subunit was simulated by N-benzylsulfonyl glycine amide or an N-acetyl D-phenylalanine amide. Single digit micromolar inhibition was found against trypsin, thrombin, Factor Xa, and Factor XIa for some analogs.

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