scholarly journals Detailed Protocols for the Selection of Antiviral Human Antibodies from Combinatorial Immune Phage Display Libraries

2018 ◽  
Author(s):  
Philipp Diebolder ◽  
Adalbert Krawczyk
Keyword(s):  
Phage Display ◽  
Human Antibodies ◽  
Phage Display Libraries ◽  
Selection Of

Selection of Human Antibodies from Phage Display Libraries

2004 ◽  
pp. 161-176 ◽  
Author(s):  
James D. Marks ◽  
Andrew Bradbury
Keyword(s):  
Phage Display ◽  
Human Antibodies ◽  
Phage Display Libraries ◽  
Selection Of

scholarly journals Selection of Peptides Targeting Helix 31 of Bacterial 16S Ribosomal RNA by Screening M13 Phage-Display Libraries

Molecules ◽  
2011 ◽  
Vol 16 (2) ◽  
pp. 1211-1239 ◽  
Author(s):  
Tek N. Lamichhane ◽  
N. Dinuka Abeydeera ◽  
Anne-Cécile E. Duc ◽  
Philip R. Cunningham ◽  
Christine S. Chow
Keyword(s):  
Phage Display ◽  
Ribosomal Rna ◽  
16S Ribosomal Rna ◽  
Phage Display Libraries ◽  
M13 Phage ◽  
Selection Of

[29] Design and use of phage display libraries for the selection of antibodies and enzymes

2000 ◽  
pp. 480-505 ◽  
Author(s):  
Francesca Viti ◽  
Fredrik Nilsson ◽  
Salvatore Demartis ◽  
Adrian Huber ◽  
Dario Neri
Keyword(s):  
Phage Display ◽  
Phage Display Libraries ◽  
Selection Of

87 Selection of pre-invasive lung cancer binding peptides using random phage display libraries

2004 ◽  
Vol 2 (8) ◽  
pp. 29
Author(s):  
J.Y. Hung ◽  
A.J. Rebello ◽  
S. Lam ◽  
J.C. Ieriche
Keyword(s):  
Lung Cancer ◽  
Phage Display ◽  
Phage Display Libraries ◽  
Binding Peptides ◽  
Selection Of

The role of valency in the selection of anti-carbohydrate single-chain Fvs from phage display libraries

1998 ◽  
Vol 220 (1-2) ◽  
pp. 39-49 ◽  
Author(s):  
Roger MacKenzie ◽  
Rebecca To
Keyword(s):  
Phage Display ◽  
Single Chain ◽  
Phage Display Libraries ◽  
Selection Of

Phage Display as A Bio-Technique for Cancer Immunotherapy

2020 ◽  
Vol 17 (4) ◽  
pp. 379-387
Author(s):  
Shirin Mahmoodi ◽  
Navid Nezafat ◽  
Younes Ghasemi
Keyword(s):  
Phage Display ◽  
Cancer Immunotherapy ◽  
Tumor Antigens ◽  
High Affinity ◽  
Phage Antibodies ◽  
Phage Display Libraries ◽  
Antigen Presenting ◽  
Immunogenic Properties ◽  
Specific Peptide ◽  
Selection Of

Background: Phage display is a biotechnological technique that presents peptides with coated proteins on the surface of phage. In the last two decades, growing applications of phage display in various fields of biotechnology have been investigated. Phage display libraries allow to present billions of peptides on phage surface for selection of a specific peptide with the desired affinity. Objective: In this regard, high-affinity phage antibodies against tumor antigens are produced and applied for diagnosis and treatment of cancer. Method: Moreover, phage display libraries are employed to select the high affinity T Cell Receptors (TCRs) for the peptide-MHC complex which is an attractive approach in cancer immunotherapy. Due to immunogenic properties of phage particles, phage-based vaccines do not require adjuvant, in addition the phage particles can effectively take up by Antigen Presenting Cells (APCs). Results: Taken together, phage-based cancer vaccines are ideal candidates that provide a key for eradication of tumor cells. Conclusion: In this review, we focus on various applications of a phage display platform in different types of cancer immunotherapy approaches.

Retrieval of human antibodies from phage-display libraries using enzymatic cleavage

1996 ◽  
Vol 189 (1) ◽  
pp. 73-82 ◽  
Author(s):  
R.L. Ward ◽  
M.A. Clark ◽  
J. Lees ◽  
N.J. Hawkins
Keyword(s):  
Phage Display ◽  
Enzymatic Cleavage ◽  
Human Antibodies ◽  
Phage Display Libraries

scholarly journals Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication

2017 ◽  
Vol 114 (25) ◽  
pp. 6444-6449 ◽  
Author(s):  
Anna Munke ◽  
Jonas Persson ◽  
Tanja Weiffert ◽  
Erwin De Genst ◽  
Georg Meisl ◽  
...  
Keyword(s):  
Phage Display ◽  
Amyloid Fibrils ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Nucleation Process ◽  
Single Chain ◽  
Secondary Nucleation ◽  
Single Chain Antibody ◽  
Phage Display Libraries ◽  
Selection Of

The aggregation of the amyloid β peptide (Aβ) into amyloid fibrils is a defining characteristic of Alzheimer’s disease. Because of the complexity of this aggregation process, effective therapeutic inhibitors will need to target the specific microscopic steps that lead to the production of neurotoxic species. We introduce a strategy for generating fibril-specific antibodies that selectively suppress fibril-dependent secondary nucleation of the 42-residue form of Aβ (Aβ42). We target this step because it has been shown to produce the majority of neurotoxic species during aggregation of Aβ42. Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation. By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process. Our method also makes it possible to discard antibodies that inhibit elongation, an important factor because the suppression of elongation does not target directly the production of toxic oligomers and may even lead to its increase. On the basis of our results, we suggest that the method described here could form the basis for rationally designed immunotherapy strategies to combat Alzheimer’s and related neurodegenerative diseases.

Sign in / Sign up

Export Citation Format

Share Document