Supramolecular design for multivalent interaction: maltose mobility along polyrotaxane enhanced binding with concanavalin A.
High molecular mobility of maltose-conjugated alpha-cyclodextrins (alpha-CDs) along a poly(ethylene glycol) (PEG) chain due to the mechanically locked structure of polyrotaxanes enhanced multivalent interactions between maltose and concanavalin A (Con A). When maltose groups are conjugated with alpha-CDs that were threaded onto a PEG capped with benzyloxycarbonyl l-tyrosine (polyrotaxane), Con A-induced hemagglutination was greatly inhibited by polyrotaxanes with a certain threading % of alpha-CDs. Such an inhibitory effect was significantly superior to the other type of conjugates, in which poly(acrylic acid) was used as a backbone for maltose conjugation. The spin-spin relaxation time (T2) of the maltose C(1) proton in the polyrotaxane at a typical alpha-CD threading % was significantly larger than that of any other conjugate, which was well related to the inhibitory effect. Therefore, we concluded that the high mobility of maltose groups along the polyrotaxane structure contributes to enhanced Con A recognition.
Ooya
Tooru
T
School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan.
Eguchi
Masaru
M
Yui
Nobuhiko
N
D003208:Concanavalin A / Q000737:chemistry* / Q000378:metabolism; D003505:Cyclodextrins / Q000737:chemistry* / Q000494:pharmacology; D006385:Hemagglutination Inhibition Tests; D008320:Maltose / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D020442:Poloxamer / Q000737:chemistry* / Q000494:pharmacology; D011485:Protein Binding; D011952:Receptors, Concanavalin A / Q000737:chemistry; D043862:Rotaxanes; D047391:alpha-Cyclodextrins
D003505:Cyclodextrins; D011952:Receptors, Concanavalin A; D043862:Rotaxanes; D047391:alpha-Cyclodextrins; C475673:polyrotaxane; D020442:Poloxamer; D003208:Concanavalin A; D008320:Maltose; C032613:alpha-cyclodextrin