Binding of β-amyloid to sulfated sugar residues in a polymer brush.
A glycopolymer obtained by living radical polymerization of glucose-carrying vinyl monomer was sulfated and accumulated as a polymer brush on a gold colloid-immobilized glass. Binding processes of various proteins to sulfated glucose residues in the brush were examined by the increase in absorbance with a help of localized surface plasmon resonance. β-Amyloid protein (Aβ) bound to the sulfated glycopolymer brush, whereas no binding to the non-sulfated one. An AFM image of Aβ aggregates on the sulfated brush was ellipsoidal, whereas no-shaped aggregation of Aβ on the poly(methacrylic acid) and poly[2-(dimethylamino)ethyl methacrylate] brushes. The present results indicate the importance of balance between electrostatic attraction and repulsion in the folding-aggregation phenomena of Aβ at the surface of glycopolymers.
Department of Applied Chemistry, Graduate School of Science and Engineering, University of Toyama, Toyama, Japan. kitano@eng.u-toyama.ac.jp
Hiromi
H
Kitano
Daisuke
D
Saito
Tomohiro
T
Kamada
Makoto
M
Gemmei-Ide
D000327:Adsorption; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D005898:Glass / Q000737:chemistry; D005947:Glucose / Q000737:chemistry*; D017979:Gold Colloid / Q000737:chemistry; D006801:Humans; D008689:Methacrylates / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D015394:Molecular Structure; D058105:Polymerization; D011108:Polymers / Q000737:chemistry*; D011485:Protein Binding; D017510:Protein Folding; D055672:Static Electricity; D013431:Sulfates; D020349:Surface Plasmon Resonance; D013499:Surface Properties
D016229:Amyloid beta-Peptides; D017979:Gold Colloid; D008689:Methacrylates; D011108:Polymers; D013431:Sulfates; D005947:Glucose