Cited by 344Cell Adhesion Molecules ResearchBiochemical and Structural CharacterizationPolymer Surface Interaction Studies

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Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library.

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Koivunen, E, Gay, D.A., Ruoslahti, E·1993·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(20)80715-7

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Abstract

The alpha 5 beta 1 integrin binds fibronectin through the integrin recognition sequence Arg-Gly-Asp (RGD). We have used a 6-amino acid peptide library expressed on filamentous phage to identify peptide ligands for alpha 5 beta 1. We found that this integrin selectively binds RGD-containing peptides from the library. Of the 32 different sequences obtained, 28 had the RGD motif, 3 contained sequences related to RGD, and only 1 had a clearly different sequence. One of the RGD-containing phage encoded a potentially cyclic insert CRGDCL. The cyclic peptide GAC*RGDC*LGA (where * denotes cysteines forming a disulfide bond) was 10-fold more efficient than any of the linear RGD-containing hexapeptides in inhibiting the binding of RGD-expressing phage to alpha 5 beta 1 or the attachment of alpha 5 beta 1-expressing cells to fibronectin. This peptide also inhibited cell attachment mediated by the alpha v beta 1, alpha v beta 3, and alpha v beta 5 integrins with about 10-fold higher efficiency than linear GRGDSP. One peptide containing an RGD-related sequence, NGRAHA, was also found to inhibit phage attachment and cell adhesion, especially adhesion mediated by the alpha v beta 5 integrin. These results indicate that novel and high affinity ligands for integrins can be isolated from a random peptide library.

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Authors: Koivunen, E., Gay, D. A., & Ruoslahti, E.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
ORCID: Koivunen, E
Ruoslahti, E
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1993-09
Volume: 268
Issue: 27
Pages: 20205-20210
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(20)80715-7
OpenAlex: W1506729263
Cited by: 344
References: 62
Citations by year: 2026: 2 · 2025: 6 · 2024: 4 · 2023: 8 · 2022: 3 · 2021: 8 · 2020: 5 · 2019: 2 · 2018: 6 · 2017: 8 · 2016: 15 · 2015: 8 · 2014: 9 · 2013: 11 · 2012: 14
FWCI: 7.09
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9883 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01ca028896-15, 5r35ca042507-07)
National Cancer Institute (CA30199, CA 28896, CA-42507, P30CA030199)
Topics: Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
Keywords: alpha5beta1 integrin, RGD peptide, fibronectin, integrin ligands, cyclic RGD peptide, phage display, cell adhesion, peptide library screening
MeSH terms: Amino Acid Sequence, Animals, Bacteriophages, Base Sequence, Binding, Competitive, Fibronectins, Cricetinae, Kinetics, Molecular Sequence Data, Oligodeoxyribonucleotides, Oligopeptides, Transfection, Gene Library, Integrins, Polymerase Chain Reaction, Databases, Factual, CHO Cells, Receptors, Fibronectin

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Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library.

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