title: A chemically modified glass surface that facilitates transglutaminase-mediated protein immobilization.
abstract: An amino-modified glass surface for enzymatic protein immobilization by microbial transglutaminase (MTG) was developed. Diamine substrates with secondary amino groups in the linker moiety, like triethylenetetramine (TETA), exhibited at most a 2-fold higher reactivity in the MTG-catalyzed reaction compared to those with the alkyl linker. A 96-well glass plate was subsequently modified with selected diamine substrates. Validation of the modified surface by enzymatic immobilization of enhanced green fluorescent protein tagged with a glutamine donor-substrate peptide (LLQG) of MTG revealed that the protein loading onto the TETA-modified glass surface was approximately 15-fold higher than that on the unmodified one.
authors.affiliation: Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka, 819-0395, Japan.
authors.forename: Yusuke
authors.initials: Y
authors.lastname: Tanaka
authors.forename: Satoshi
authors.initials: S
authors.lastname: Doi
authors.forename: Noriho
authors.initials: N
authors.lastname: Kamiya
authors.forename: Noriyuki
authors.initials: N
authors.lastname: Kawata
authors.forename: Shinji
authors.initials: S
authors.lastname: Kamiya
authors.forename: Kenichi
authors.initials: K
authors.lastname: Nakama
authors.forename: Masahiro
authors.initials: M
authors.lastname: Goto
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D002384:Catalysis; D005898:Glass / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D013499:Surface Properties; D011503:Transglutaminases / Q000378:metabolism*; D014266:Trientine / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; D011503:Transglutaminases; D014266:Trientine