Peptides binding to a Gb3 mimic selected from a phage library.
Peptides binding to a Gb3 mimic were selected from 12-mer peptide library. The self-assembled monolayer (SAM) of a Gb3 mimic was formed on the gold surface, and biopanning was carried out with the phage display peptide library. After three rounds of biopanning, four individual sequences were obtained from 10 phage clones, and the selected peptides having the specific 7-mer sequence (FHENWPS) showed affinities to the Gb3 mimic as strong as to RCA120. Molecular dynamics calculations suggested that the peptides bound to the Gb3 mimic by hydrophobic interaction and hydrogen bonding formation, and the cooperative interactions played an important role in the recognition. The Stx-1 binding was inhibited by the peptides.
Department of Molecular Design and Engineering, Graduate School of Engineering, Nagoya University, Chikusa, Nagoya 464-8603, Japan. miuray@mol.nagoya-u.ac.jp
Yoshiko
Y
Miura
Yuuki
Y
Sasao
Masamichi
M
Kamihira
Akio
A
Sakaki
Shinji
S
Iijima
Kazukiyo
K
Kobayashi
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000378:metabolism*; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D014281:Trihexosylceramides / Q000737:chemistry / Q000378:metabolism*
D010455:Peptides; D014281:Trihexosylceramides; C018549:globotriaosylceramide