Crystal structure and NMR investigation of the serine proteinase inhibitor MR889, a cyclic thiolic compound

Menico Rizzi, Elena Casale, Paolo Ascenzi, Mauro Fasano, Silvio Aime, Concetta La Rosa, Maurizio Luisetti, Martino Bolognesi

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Abstract

The serine proteinase inhibitor N-(2-oxo-2,3,4,5-tetrahydro-3-thienyl)-2- (2-thenoylthio)propionamide (MR889) has been crystallised, and its three-dimensional structure studied by X-ray diffraction and by NMR techniques in solution and in the solid state. MR889 crystallises in the monoclinic space group P21/n with cell constants a = 10.539(2), b = 9.647(5), c= 14.654(1) Å, β = 101.62(1)°; the asymmetric unit contains one molecule of MR889. The weighted crystallographic R factor for the refined structure is 0.044. The solution structure of MR889 has been elucidated through the measurement of proton-proton and proton-carbon nuclear Overhauser enhancements. Measurement of the 13C longitudinal relaxation times yields information about the dynamics of MR889 in dimethylsulfoxide solution. The comparison between solid and solution state 13C NMR spectra allows an understanding of the quite different structures in the two states.

Original languageEnglish
Pages (from-to)2253-2256
Number of pages4
JournalJournal of the Chemical Society, Perkin Transactions 2
Issue number11
Publication statusPublished - 1993

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ASJC Scopus subject areas

  • Chemistry(all)

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Rizzi, M., Casale, E., Ascenzi, P., Fasano, M., Aime, S., La Rosa, C., Luisetti, M., & Bolognesi, M. (1993). Crystal structure and NMR investigation of the serine proteinase inhibitor MR889, a cyclic thiolic compound. Journal of the Chemical Society, Perkin Transactions 2, (11), 2253-2256.