Selection of Antagonists of Fibroblast Growth Factor from a Phage-Display Peptide Library

2001 ◽  
pp. 927-928
Author(s):  
Hongkuan Fan ◽  
Hui Zhou ◽  
Wei Li ◽  
Roger W. Roeske ◽  
Lili Guo
Keyword(s):  
Growth Factor ◽  
Phage Display ◽  
Fibroblast Growth Factor ◽  
Peptide Library ◽  
Fibroblast Growth ◽  
Phage Display Peptide Library ◽  
Selection Of

scholarly journals Selection of Peptide Ligands That Bind to Acid Fibroblast Growth Factor

IUBMB Life ◽  
2000 ◽  
Vol 49 (6) ◽  
pp. 545-548 ◽  
Author(s):  
Hongkuan Fan, Ying Liu, Hui Zhou, Liping Wan
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Peptide Ligands ◽  
Fibroblast Growth ◽  
Selection Of

scholarly journals Novel Method for Selection of Antimicrobial Peptides from a Phage Display Library by Use of Bacterial Magnetic Particles

2008 ◽  
Vol 74 (24) ◽  
pp. 7600-7606 ◽  
Author(s):  
Tsuyoshi Tanaka ◽  
Yoriko Kokuryu ◽  
Tadashi Matsunaga
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Phage Display ◽  
Magnetic Particles ◽  
Peptide Library ◽  
Inner Membrane ◽  
Phage Display Peptide Library ◽  
Wide Range ◽  
Bacterial Magnetic Particles ◽  
Selection Of

ABSTRACT Antimicrobial peptides were isolated from a phage display peptide library using bacterial magnetic particles (BacMPs) as a solid support. The BacMPs obtained from “Magnetospirillum magneticum” strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane. BacMPs are easily purified from a culture of magnetotactic bacteria by magnetic separation. Approximately 4 × 1010 PFU of the library phage (complexity, 2.7 × 109) was reacted with BacMPs. The elution of bound phages from BacMPs was performed by disrupting its membrane with phospholipase D treatment. Six candidate peptides, which were highly cationic and could bind onto the BacMP membrane, were obtained. They exhibited antimicrobial activity against Bacillus subtilis but not against Escherichia coli and Saccharomyces cerevisiae. The amino acid substitution of the selected peptide, KPQQHNRPLRHK (peptide 6-7), to enhance the hydrophobicity resulted in obvious antimicrobial activity against all test microorganisms. The present study shows for the first time that a magnetic selection of antimicrobial peptides from the phage display peptide library was successfully achieved by targeting the actual bacterial inner membrane. This BacMP-based method could be a promising approach for a high-throughput screening of antimicrobial peptides targeting a wide range of species.

scholarly journals Selection of Peptide Ligands Binding to Fibroblast Growth Factor Receptor 1

IUBMB Life ◽  
2002 ◽  
Vol 54 (2) ◽  
pp. 67-72 ◽  
Author(s):  
Hongkuan Fan ◽  
Hui Zhou ◽  
Wei Li ◽  
Fei Li ◽  
Lili Guo ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Peptide Ligands ◽  
Fibroblast Growth ◽  
Selection Of

Conformational Selection of the AGA*IAM Heparin Pentasaccharide when Bound to the Fibroblast Growth Factor Receptor

2011 ◽  
Vol 17 (40) ◽  
pp. 11204-11209 ◽  
Author(s):  
Lidia Nieto ◽  
Ángeles Canales ◽  
Guillermo Giménez-Gallego ◽  
Pedro M. Nieto ◽  
Jesús Jiménez-Barbero
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth ◽  
Conformational Selection ◽  
Selection Of

Selection of CC Chemokine Receptor 5-Binding Peptide from a Phage Display Peptide Library

2006 ◽  
Vol 70 (9) ◽  
pp. 2035-2041 ◽  
Author(s):  
Fang-Yu WANG ◽  
Tian-Yuan ZHANG ◽  
Jin-Xian LUO ◽  
Guo-An HE ◽  
Qu-Liang GU ◽  
...  
Keyword(s):  
Phage Display ◽  
Chemokine Receptor ◽  
Peptide Library ◽  
Binding Peptide ◽  
Cc Chemokine ◽  
Phage Display Peptide Library ◽  
Cc Chemokine Receptor 5 ◽  
Selection Of ◽  
Chemokine Receptor 5

scholarly journals Identification of Novel Single-Domain Antibodies against FGF7 Using Phage Display Technology

2017 ◽  
Vol 23 (2) ◽  
pp. 193-201
Author(s):  
Behzad Jafari ◽  
Maryam Hamzeh-Mivehroud ◽  
Ali A. Moosavi-Movahedi ◽  
Siavoush Dastmalchi
Keyword(s):  
Growth Factor ◽  
Phage Display ◽  
Fibroblast Growth Factor ◽  
Single Domain ◽  
Enzyme Linked Immunosorbent Assay ◽  
Fibroblast Growth ◽  
Phage Display Technology ◽  
Display Technology ◽  
Single Domain Antibodies

Fibroblast growth factor 7 (FGF7) is a member of the fibroblast growth factor (FGF) family of proteins. FGF7 is of stromal origin and produces a paracrine effect on epithelial cells. In the current investigation, we aimed to identify new single-domain antibodies (sdAbs) against FGF7 using phage display technology. The vector harboring the codon-optimized DNA sequence for FGF7 protein was transformed into Escherichia coli BL21 (DE3) pLysS, and then the protein was expressed at the optimized condition. Enzyme-linked immunosorbent assay, circular dichroism spectropolarimetry, and in vitro scratch assay experiments were used to confirm the proper folding and functionality of the purified FGF7 protein. The purity of the produced FGF7 was 92%, with production yield of 3.5 mg/L of culture. Panning against the purified FGF7 was performed, and the identified single-domain antibodies showed significant affinity. Further investigation on one of the selected sdAb displaying phage clones showed concentration-dependent binding to FGF7. The selected sdAb can be used for developing novel tumor-suppressing agents where inhibition of FGF7 is required.

Plasmonic Selection of ssDNA Aptamers against Fibroblast Growth Factor Receptor

2019 ◽  
Vol 21 (8) ◽  
pp. 578-587 ◽  
Author(s):  
Hasan Kurt ◽  
Alp Ertunga Eyüpoğlu ◽  
Tolga Sütlü ◽  
Hikmet Budak ◽  
Meral Yüce
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth ◽  
Selection Of

Isolation and preliminary characterization of a human ‘phage display’-derived antibody against neural adhesion molecule-1 antigen interfering with fibroblast growth factor receptor-1 binding

2020 ◽  
pp. 1-22
Author(s):  
Michela Flego ◽  
Gianni Colotti ◽  
Alessandro Ascione ◽  
Maria Luisa Dupuis ◽  
Eleonora Petrucci ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Growth Factor ◽  
Phage Display ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth ◽  
Single Chain ◽  
Preliminary Characterization

BACKGROUND: The NCAM or CD56 antigen is a cell surface glycoprotein belonging to the immunoglobulin super-family involved in cell-cell and cell-matrix adhesion. NCAM is also over-expressed in many tumour types and is considered a tumour associated antigen, even if its role and biological mechanisms implicated in tumour progression and metastasis have not yet to be elucidated. In particular, it is quite well documented the role of the interaction between the NCAM protein and the fibroblast growth factor receptor-1 in metastasis and invasion, especially in the ovarian cancer progression. OBJECTIVE: Here we describe the isolation and preliminary characterization of a novel human anti-NCAM single chain Fragment variable antibody able to specifically bind NCAM-expressing cells, including epithelial ovarian cancer cells. METHODS: The antibody was isolate by phage display selection and was characterized by ELISA, FACS analysis and SPR experiments. Interference in EOC migration was analyzed by scratch test. RESULTS: It binds a partially linear epitope lying in the membrane proximal region of two fibronectin-like domains with a dissociation constant of 3.43 × 10-8 M. Interestingly, it was shown to interfere with the NCAM-FGFR1 binding and to partially decrease migration of EOC cells. CONCLUSIONS: According to our knowledge, this is the first completely human antibody able to interfere with this newly individuated cancer mechanism.

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