Diastereomeric Glycosyl Sulfoxides Display Different Recognition Features versus E. coli β-Galactosidase

  1. Colomer, J.P. 2
  2. Fernández de Toro, B. 4
  3. Cañada, F.J. 4
  4. Corzana, F. 5
  5. Jiménez Barbero, J. 137
  6. Canales, Á. 6
  7. Varela, Oscar . 2
  1. 1 Centro de Investigación Cooperativa en Biotecnología
    info

    Centro de Investigación Cooperativa en Biotecnología

    Zamudio, España

  2. 2 Universidad de Buenos Aires
    info

    Universidad de Buenos Aires

    Buenos Aires, Argentina

    ROR https://ror.org/0081fs513

  3. 3 Universidad del País Vasco/Euskal Herriko Unibertsitatea
    info

    Universidad del País Vasco/Euskal Herriko Unibertsitatea

    Lejona, España

    ROR https://ror.org/000xsnr85

  4. 4 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  5. 5 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  6. 6 Universidad Complutense de Madrid
    info

    Universidad Complutense de Madrid

    Madrid, España

    ROR 02p0gd045

  7. 7 IKERBASQUE, Basque Foundation for Science, Bilbao, Spain
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Revista:
European Journal of Organic Chemistry

ISSN: 1434-193X

Any de publicació: 2016

Volum: 2016

Número: 30

Pàgines: 5117-5122

Tipus: Article

DOI: 10.1002/EJOC.201600835 SCOPUS: 2-s2.0-84990872400 WoS: WOS:000386919600006 GOOGLE SCHOLAR

Altres publicacions en: European Journal of Organic Chemistry

Objectius de Desenvolupament Sostenible

Resum

The conformational analysis of the (S) and (R) diastereoisomers of benzyl 3-deoxy-4S-(β-d-galactopyranosyl)-4-thio-β-d-threo-pentopyranoside S-oxide (1S and 1R, respectively) has been performed by using NMR spectroscopy assisted by molecular modelling methods. The results point out that sulfoxide 1S and 1R display rather different conformational behaviors, 1S being significantly more flexible than 1R. Both sulfoxides have shown to be competitive inhibitors of the β-galactosidase from E. coli, although with different potencies. The key structural features of the molecular recognition process have been characterized. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim