Cellulose-binding heptapeptides identified by phage display methods

Takeshi Serizawa; Kyoko Iida; Hisao Matsuno; Kimio Kurita

doi:10.1246/cl.2007.988

Cellulose-binding heptapeptides identified by phage display methods

Takeshi Serizawa, Kyoko Iida, Hisao Matsuno, Kimio Kurita

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

Phage libraries displaying random and linear heptapeptides were applied to crystalline cellulose. Binding affinities of obtained phage clones were quantitatively analyzed by enzyme-linked immunosorbent assays (ELISAs). Clones were obtained with greater apparent affinity constants (K_apps) than those of the library, suggesting the isolation of cellulose-binding peptides with characteristic sequences.

Original language	English
Pages (from-to)	988-989
Number of pages	2
Journal	Chemistry Letters
Volume	36
Issue number	8
DOIs	https://doi.org/10.1246/cl.2007.988
Publication status	Published - Aug 5 2007
Externally published	Yes

All Science Journal Classification (ASJC) codes

Chemistry(all)

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10.1246/cl.2007.988

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title = "Cellulose-binding heptapeptides identified by phage display methods",

abstract = "Phage libraries displaying random and linear heptapeptides were applied to crystalline cellulose. Binding affinities of obtained phage clones were quantitatively analyzed by enzyme-linked immunosorbent assays (ELISAs). Clones were obtained with greater apparent affinity constants (Kapps) than those of the library, suggesting the isolation of cellulose-binding peptides with characteristic sequences.",

author = "Takeshi Serizawa and Kyoko Iida and Hisao Matsuno and Kimio Kurita",

year = "2007",

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AU - Serizawa, Takeshi

AU - Iida, Kyoko

AU - Matsuno, Hisao

AU - Kurita, Kimio

PY - 2007/8/5

Y1 - 2007/8/5

N2 - Phage libraries displaying random and linear heptapeptides were applied to crystalline cellulose. Binding affinities of obtained phage clones were quantitatively analyzed by enzyme-linked immunosorbent assays (ELISAs). Clones were obtained with greater apparent affinity constants (Kapps) than those of the library, suggesting the isolation of cellulose-binding peptides with characteristic sequences.

AB - Phage libraries displaying random and linear heptapeptides were applied to crystalline cellulose. Binding affinities of obtained phage clones were quantitatively analyzed by enzyme-linked immunosorbent assays (ELISAs). Clones were obtained with greater apparent affinity constants (Kapps) than those of the library, suggesting the isolation of cellulose-binding peptides with characteristic sequences.

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DO - 10.1246/cl.2007.988

M3 - Article

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SP - 988

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JO - Chemistry Letters

JF - Chemistry Letters

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ER -

Cellulose-binding heptapeptides identified by phage display methods

Abstract

All Science Journal Classification (ASJC) codes

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