Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

10.3791/60189 ◽  
2019 ◽  
Author(s):  
Ying Zhao ◽  
Qiang Wang ◽  
An Hong ◽  
Xiaojia Chen
Keyword(s):  
Growth Factor ◽  
Phage Display ◽  
Fibroblast Growth Factor ◽  
Peptide Library ◽  
Fibroblast Growth ◽  
Small Peptides ◽  
Phage Display Peptide Library ◽  
Screening And Identification

Screening and Identification of a peptide specifically targeted to NCI-H1299 from a phage display peptide library

2009 ◽  
Vol 281 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Linquan Zang ◽  
Lei Shi ◽  
Jiao Guo ◽  
Qin Pan ◽  
Wei Wu ◽  
...  
Keyword(s):  
Phage Display ◽  
Peptide Library ◽  
Phage Display Peptide Library ◽  
Screening And Identification

scholarly journals Screening and Identification of a Targeting Peptide to Hepatocarcinoma from a Phage Display Peptide Library

2007 ◽  
Vol 13 (5-6) ◽  
pp. 246-254 ◽  
Author(s):  
Binghua Zhang ◽  
Yanqiong Zhang ◽  
Jiwei Wang ◽  
Yangde Zhang ◽  
Jiji Chen ◽  
...  
Keyword(s):  
Phage Display ◽  
Peptide Library ◽  
Phage Display Peptide Library ◽  
Screening And Identification ◽  
Targeting Peptide

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.

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.

Sign in / Sign up

Export Citation Format

Share Document