Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 131-138 |
| Number of pages | 8 |
| Journal | Biochimica et Biophysica Acta - General Subjects |
| Volume | 1673 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Aug 4 2004 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
Cite this
Peptides binding to a Gb3 mimic selected from a phage library. / Miura, Yoshiko; Sasao, Yuuki; Kamihira, Masamichi; Sakaki, Akio; Iijima, Shinji; Kobayashi, Kazukiyo.
In: Biochimica et Biophysica Acta - General Subjects, Vol. 1673, No. 3, 04.08.2004, p. 131-138.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Peptides binding to a Gb3 mimic selected from a phage library
AU - Miura, Yoshiko
AU - Sasao, Yuuki
AU - Kamihira, Masamichi
AU - Sakaki, Akio
AU - Iijima, Shinji
AU - Kobayashi, Kazukiyo
PY - 2004/8/4
Y1 - 2004/8/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=3242797310&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3242797310&partnerID=8YFLogxK
U2 - 10.1016/j.bbagen.2004.04.009
DO - 10.1016/j.bbagen.2004.04.009
M3 - Article
C2 - 15279884
AN - SCOPUS:3242797310
VL - 1673
SP - 131
EP - 138
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 3
ER -