Alpha-rhamnosidase inhibitory activities of polyhydroxylated pyrrolidine

Bioorg Med Chem Lett. 2005 Oct 1;15(19):4282-5. doi: 10.1016/j.bmcl.2005.06.051.

Abstract

We designed and synthesized polyhydroxylated pyrrolidines 1-12 from L-tyrosine, L-phenylalanine, and D-tyrosine through iodine-mediated intramolecular cyclization followed by Woodward-Prevost reaction. The synthetic polyhydroxylated pyrrolidines were identified with structure-based inhibitory activity and selective inhibitory activity against alpha-rhamnosidase. (2S,3S,4R)-deacetyl anisomycin 7 was the best inhibitor among the 12 polyhydroxylated pyrrolidines because it possesses the same stereoconfiguration at C1, C2, C3 as alpha-L-rhamnopyranoside. An investigation into the nature of the inhibition showed that the synthetic pyrrolidines are competitive inhibitors. They also did not have remarkable inhibitory activity against seven glycosidases (alpha-glucosidase, alpha-mannosidase, alpha-amylase, beta-glucosidase, beta-galactosidase, beta-amylase, and invertase).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry
  • Anisomycin / chemical synthesis
  • Anisomycin / pharmacology
  • Binding, Competitive
  • Cyclization
  • Glycoside Hydrolases / antagonists & inhibitors*
  • Glycoside Hydrolases / metabolism
  • Hydroxylation
  • Inhibitory Concentration 50
  • Pyrrolidines / chemical synthesis*
  • Pyrrolidines / pharmacology
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Pyrrolidines
  • Anisomycin
  • Glycoside Hydrolases
  • alpha-L-rhamnosidase
  • pyrrolidine