Probing bacterial-toxin inhibition with synthetic glycopolymers prepared by tandem post-polymerization modification: role of linker length and carbohydrate density.
Probing the depths: A tandem post-polymerization modification strategy was used to systematically probe the multivalent inhibition of a bacterial toxin as a function of linker length (see scheme), carbohydrate density, and glycopolymer chain length. Guided by structural-biology information, the binding-pocket depth of the toxin was probed and used as a means to specifically improve inhibition of the toxin by the glycopolymer.
Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.
Sarah-Jane
SJ
Richards
Mathew W
MW
Jones
Mark
M
Hunaban
David M
DM
Haddleton
Matthew I
MI
Gibson
D001665:Binding Sites / Q000187:drug effects; D002772:Cholera Toxin / Q000737:chemistry / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D037102:Lectins / Q000037:antagonists & inhibitors* / Q000737:chemistry; D015394:Molecular Structure; D019887:Peanut Agglutinin / Q000737:chemistry / Q000494:pharmacology*; D058105:Polymerization; D011134:Polysaccharides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014734:Vibrio cholerae / Q000737:chemistry*
D037102:Lectins; D019887:Peanut Agglutinin; D011134:Polysaccharides; D002772:Cholera Toxin