title: Functionalized carbon nanotubes specifically bind to alpha-chymotrypsin's catalytic site and regulate its enzymatic function.
abstract: Although carbon nanotubes (CNTs) have been shown to nonspecifically bind proteins through charge complementary, pi-pi stacking or hydrophobic interactions, they have not been shown to bind to a specific site on proteins. By generating surface molecular diversity, we created functionalized CNTs that recognize and bind to the catalytic site of alpha-chymotrypsin and inhibit its enzymatic activity competitively.
authors.affiliation: School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, China.
authors.forename: Bin
authors.initials: B
authors.lastname: Zhang
authors.forename: Yuehan
authors.initials: Y
authors.lastname: Xing
authors.forename: Zhenwei
authors.initials: Z
authors.lastname: Li
authors.forename: Hongyu
authors.initials: H
authors.lastname: Zhou
authors.forename: Qingxin
authors.initials: Q
authors.lastname: Mu
authors.forename: Bing
authors.initials: B
authors.lastname: Yan
mesh_terms: D020134:Catalytic Domain; D002918:Chymotrypsin / Q000737:chemistry*; D020650:Combinatorial Chemistry Techniques; D016503:Drug Delivery Systems; D005453:Fluorescence; D057927:Hydrophobic and Hydrophilic Interactions; D037742:Nanotubes, Carbon / Q000737:chemistry*
chemical_list: D037742:Nanotubes, Carbon; D002918:Chymotrypsin; C117608:alpha-chymotrypsin