scholarly journals Identification of a WSSV neutralizing scFv antibody by phage display technology and in vitro screening

2006 ◽  
Vol 72 ◽  
pp. 93-99 ◽  
Author(s):  
L Yuan ◽  
X Zhang ◽  
N Xiao ◽  
L Dai ◽  
W Chen ◽  
...  
Keyword(s):  
Phage Display ◽  
Scfv Antibody ◽  
In Vitro Screening ◽  
Phage Display Technology ◽  
Display Technology

scholarly journals Novel Blood–Brain Barrier Shuttle Peptides Discovered through the Phage Display Method

Molecules ◽  
2020 ◽  
Vol 25 (4) ◽  
pp. 874 ◽  
Author(s):  
Petra Majerova ◽  
Jozef Hanes ◽  
Dominika Olesova ◽  
Jakub Sinsky ◽  
Emil Pilipcinec ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Phage Display ◽  
Blood Brain Barrier ◽  
Brain Barrier ◽  
Phage Display Technology ◽  
Blood Brain ◽  
Display Technology ◽  
The Brain

Delivery of therapeutic agents into the brain is a major challenge in central nervous system drug development. The blood–brain barrier (BBB) prevents access of biotherapeutics to their targets in the central nervous system and, therefore, prohibits the effective treatment of many neurological disorders. To find blood–brain barrier shuttle peptides that could target therapeutics to the brain, we applied a phage display technology on a primary endothelial rat cellular model. Two identified peptides from a 12 mer phage library, GLHTSATNLYLH and VAARTGEIYVPW, were selected and their permeability was validated using the in vitro BBB model. The permeability of peptides through the BBB was measured by ultra-performance liquid chromatography-tandem mass spectrometry coupled to a triple-quadrupole mass spectrometer (UHPLC-MS/MS). We showed higher permeability for both peptides compared to N–C reversed-sequence peptides through in vitro BBB: for peptide GLHTSATNLYLH 3.3 × 10−7 cm/s and for peptide VAARTGEIYVPW 1.5 × 10−6 cm/s. The results indicate that the peptides identified by the in vitro phage display technology could serve as transporters for the administration of biopharmaceuticals into the brain. Our results also demonstrated the importance of proper BBB model for the discovery of shuttle peptides through phage display libraries.

In vitro effect of a thrombin inhibition peptide selected by phage display technology

2002 ◽  
Vol 107 (6) ◽  
pp. 365-371 ◽  
Author(s):  
Muriel S Meiring ◽  
Derek Litthauer ◽  
Jolan Hársfalvi ◽  
Veronica van Wyk ◽  
Philip N Badenhorst ◽  
...  
Keyword(s):  
Phage Display ◽  
Phage Display Technology ◽  
Thrombin Inhibition ◽  
Display Technology ◽  
Vitro Effect

scholarly journals A novel, stable, helical scaffold as an alternative binder - construction of phage display libraries.

2012 ◽  
Vol 59 (3) ◽  
Author(s):  
Anna Cyranka-Czaja ◽  
Jacek Otlewski
Keyword(s):  
Phage Display ◽  
Measles Virus ◽  
In Vitro Selection ◽  
Biophysical Properties ◽  
Phage Display Technology ◽  
High Affinity ◽  
Promising Tool ◽  
Phage Display Libraries ◽  
Display Technology

Specific, high affinity binding macromolecules are of great importance for biomedical and biotechnological applications. The most popular classical antibody-based molecules have recently been challenged by alternative scaffolds with desirable biophysical properties. Phage display technology applied to such scaffolds allows generation of potent affinity reagents by in vitro selection. Here, we report identification and characterization of a novel helical polypeptide with advantageous biophysical properties as a template for construction of phage display libraries. A three-helix bundle structure, based on Measles virus phosphoprotein P shows a very favourable stability and solubility profile. We designed, constructed and characterized six different types of phage display libraries based on the proposed template. Their functional size of over 10(9) independent clones, balanced codon bias and decent display level are key parameters attesting to the quality and utility of the libraries. The new libraries are a promising tool for isolation of high affinity binders based on a small helical scaffold which could become a convenient alternative to antibodies.

scholarly journals Isolation of a novel Anti-KDR3 Single-chain Variable Fragment Antibody from a Phage Display Library

2019 ◽  
Author(s):  
Shirafkan Kordi ◽  
Mohammad Rahmati-Yamchi ◽  
Mehdi Asghari Vostakolaei ◽  
Ali Etemadie ◽  
Abolfazl Barzegari ◽  
...  
Keyword(s):  
Phage Display ◽  
Growth Factor Receptor ◽  
Phage Display Library ◽  
Vital Role ◽  
Scfv Antibody ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Phage Display Technology ◽  
Display Technology ◽  
Domain 3

Vascular endothelial growth factor receptor 2 (VEGFR-2) is known as one of the important antigens playing a vital role in angiogenesis. In this study, phage display technology (PDT) was used to produce a single-chain variable fragment (scFv) antibody against a region of the domain 3 in VEGFR-2 called kinase insert domain receptor 3 (KDR3). After designing the KDR3 peptide and biopanning, a colony was chosen for scFv antibody expression. Following expression and purification; western blotting, dot blotting and immunofluorescence (IF) were used to evaluate the antibody function. Surface plasmon resonance (SPR) was also employed to measure affinity of produced antibody. Once a colony was selected and transferred to the expression host, the scFv antibody was expressed in the expected range of 28 kDa. Using a designed chromatography column, antibody purification was found to be about 95%. In this study, a novel scFv with the capability of binding to KDR3 was isolated and purified and its intracellular function was investigated and verified.

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.

scholarly journals Pretargeted cancer radioimmunotherapy and radioimaging using antibodies and antibody fragments

2018 ◽  
Author(s):  
◽  
Manankumar Shah
Keyword(s):  
Phage Display ◽  
Therapeutic Index ◽  
Single Chain ◽  
Cell Binding ◽  
Phage Display Technology ◽  
Good Target ◽  
Display Technology ◽  
Cell To Cell Adhesion ◽  
Radiolabeled Antibodies

Over the last few decades, antibodies have become the mainstay of cancer diagnosis and therapeutics. In traditional radioimmunotherapy (RIT), tumor targeting antibodies are directly conjugated with radioisotopes and depending on the radionuclides's properties, the direct labeled antibodies can be used for diagnostic or therapeutic purposes. However, one of the major challenges of using radiolabeled antibodies for therapy is their long serum half-lives. It generally takes 5-7 days for antibodies to achieve maximum tumor binding. This slow blood clearance results in high normal tissue irradiation and a poor therapeutic index. This is exemplified by the fact that to date, only two radiolabeled antibodies have been approved by the FDA for radioimmunotherapy of cancer. … Thomsen-Friedenreich (TF) is a disaccharide (Galactose [beta]1-3 N-acetylgalactosamine) antigen, which is present on about [about]90% of carcinomas. The TF expression on the tumor cell is correlated with poor prognosis and tumor propagation. TF antigen is also involved in cell to cell adhesion and metastasis, making it a very good target for cancer imaging and therapy. Using phage display technology, TF binding scFv fragments were selected from the McCafferty antibody library. The selected scFv clones were characterized in vitro for their TF specificity and cell binding properties by ELISA and flow-cytometry assay. The selected TF specific clone (9C-scFv) was radiolabeled with [99m]Tc by directly conjugating [99m]Tc to the C-terminal 6x His-tag. The [99m]Tc-labeled 9C-scFv was injected in mice bearing MDA-MB-231 human breast cancer xenografts. The SPECT/CT images, acquired 4 hours post injection, revealed a moderate tumor uptake of radiolabeled scFvs with significant accumulation in the liver and kidneys. The phage display derived single-chain scFv fragments against the TF antigen demonstrated potential for development as an imaging agent but requires more work to achieve favorable pharmacokinetics.

scholarly journals Application of Recombinant Human scFv Antibody as a Powerful Tool to Monitor Nitrogen Fixing Biofertilizer in Rice and Legume

2021 ◽  
Author(s):  
K. K. Khaing ◽  
K. Rangnoi ◽  
H. Michlits ◽  
N. Boonkerd ◽  
N. Teaumroong ◽  
...  
Keyword(s):  
Phage Display ◽  
Recombinant Antibodies ◽  
Scfv Antibody ◽  
Nitrogen Fixing ◽  
Phage Display Technology ◽  
Human Scfv ◽  
Display Technology

Human scFv antibody generated from phage display technology was successfully used for the generation of specific recombinant antibodies: yiN92-1e10 and yiDOA9-162 for the detection of Bradyrhizobium strains SUTN9-2 and DOA9, respectively.

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