Analysis of novel streptavidin-binding peptides, identified using a phage display library, shows that amino acids external to a perfectly conserved consensus sequence and to the presented peptides contribute to binding-Reference-Cited by-同舟云学术

Analysis of novel streptavidin-binding peptides, identified using a phage display library, shows that amino acids external to a perfectly conserved consensus sequence and to the presented peptides contribute to binding

Published:1996-08 Issue:4 Volume:1 Page:241-246
ISSN:1381-1991
Container-title:Molecular Diversity
language:en
Short-container-title:Mol Divers

Author:

Caparon Maire H.,De Ciechi Pamela A.,Devine Catherine S.,Olins Peter O.,Lee Stephen C.

Publisher

Springer Science and Business Media LLC

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Drug Discovery,Molecular Biology,General Medicine,Information Systems,Catalysis

Link

http://link.springer.com/content/pdf/10.1007/BF01715528.pdf

Reference19 articles.

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2. Winter, J.,Bacteriophage display: Peptide libraries and drug discovery, Drug Dev. Res., 33 (1994) 71–89.

3. O'Neil, K.T., Hoess, R.H., Jackson, S.A., Ramachandran, N.S., Mousa, S.A. and DeGrado, W.F.,Identification of novel peptide antagonists for GPIIb/IIIa from a conformationally constrained phage peptide library, Proteins, 14 (1992) 509–515.

4. Koivunen, E., Gay, D.A. and Ruosslati, E.,Selection of peptides binding to α 5 β 1 integrin from a phage display library, J. Biol. Chem., 268 (1993) 20205–20210.

5. Smith, G.P.,Surface display and peptide libraries, Gene, 128 (1993) 1–2.

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