scholarly journals Phage Display-Derived Peptide for the Specific Binding of SARS-CoV-2

ACS Omega ◽  
2021 ◽  
Author(s):  
Fan Yang ◽  
Li Liu ◽  
Pierre Fernand Neuenschwander ◽  
Steven Idell ◽  
Ramakrishna Vankayalapati ◽  
...  
Keyword(s):  
Phage Display ◽  
Specific Binding

Evidence for Autostimulatory Mechanisms in Chronic Lymphocytic Leukemia.

Blood ◽  
2012 ◽  
Vol 120 (21) ◽  
pp. 2880-2880
Author(s):  
Martin Trepel ◽  
Fabian Muller ◽  
Mareike Frick ◽  
Janina Rahlff ◽  
Claudia Wehr ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
Phage Display ◽  
B Cell ◽  
Conflicts Of Interest ◽  
Specific Binding ◽  
Variable Region ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Lymphocytic Leukemia ◽  
Fab Fragment

Abstract Abstract 2880 Background: The development and / or course of chronic lymphocytic leukemia (CLL) may be driven by the recognition of antigens through the B cell receptor (BCR). While it has been recognized that the diversity of epitope recognition may be astonishingly confined in CLL, knowledge on antigens recognized by CLL BCRs is still limited. Here, we identified and characterized an epitope recognized by a defined CLL BCR which may broaden our view on potential mechanisms of antigenic drive in CLL. Methods: The B- cell receptor of a random CLL-patient was cloned and expressed as Fab fragment in E.coli. Random phage display reptile litanies we skeletal on the immobilized Fab and landed peptides were tested for specific binding. Specific clones we sequenced and sequences were analyzed for homology to known proteins. Recognition of candidate proteins was verified in brooding assays or recombinant proteins. Results: Screening random phage display peptide libraries, we identified a CLL BCR epitope mimic that displayed a high degree of homology to a conserved peptide string in the variable region of immunoglobulin heavy and light chains. CLL BCR binding to this epitope as well as binding to full length heavy and light immunoglobulin chains was verified by binding assays and a protein array screening. Interestingly, the CLL BCR also interacted with itself, as the identified epitope was also present in its own primary amino acid sequence. Conclusions: These findings suggest the possibility of self-recognition of BCRs within the CLL cell membrane or BCR interactions between neighboring CLL cells. This may potentially result in autostimulation of the leukemic cell independent of “exogenous” antigens and may account for self-sufficient signaling of some CLL-BCRs in driving disease progression. As the peptide mimicking this immunoglobulin epitope is known to be recognized by BCRs of other CLL cases in addition to the index case investigated here, such autostimulatory mechanisms may be relevant to a large number of CLL patients. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Isolation of a Colon Tumor Specific Binding Peptide Using Phage Display Selection

Neoplasia ◽  
2003 ◽  
Vol 5 (5) ◽  
pp. 437-444 ◽  
Author(s):  
Kimberly A. Kelly ◽  
David A. Jones
Keyword(s):  
Phage Display ◽  
Specific Binding ◽  
Colon Tumor ◽  
Binding Peptide

scholarly journals Selection of single chain antibody fragments binding to the extracellular domain of 4-1BB receptor by phage display technology

Tumor Biology ◽  
2017 ◽  
Vol 39 (3) ◽  
pp. 101042831769592 ◽  
Author(s):  
Salman Bagheri ◽  
Mehdi Yousefi ◽  
Elmira Safaie Qamsari ◽  
Farhad Riazi-Rad ◽  
Mohsen Abolhassani ◽  
...  
Keyword(s):  
Phage Display ◽  
Immunosorbent Assay ◽  
Specific Binding ◽  
Interleukin 2 ◽  
Extracellular Domain ◽  
Surface Glycoprotein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Single Chain ◽  
Single Chain Variable Fragments ◽  
Selection Of

The 4-1BB is a surface glycoprotein that pertains to the tumor necrosis factor–receptor family. There is compelling evidence suggesting important roles for 4-1BB in the immune response, including cell activation and proliferation and also cytokine induction. Because of encouraging results of different agonistic monoclonal antibodies against 4-1BB in the treatment of cancer, infectious, and autoimmune diseases, 4-1BB has been suggested as an attractive target for immunotherapy. In this study, single chain variable fragment phage display libraries, Tomlinson I+J, were screened against specific synthetic oligopeptides (peptides I and II) designed from 4-1BB extracellular domain. Five rounds of panning led to selection of four 4-1BB specific single chain variable fragments (PI.12, PI.42, PII.16, and PII.29) which showed specific reaction to relevant peptides in phage enzyme-linked immunosorbent assay. The selected clones were successfully expressed in Escherichia coli Rosetta-gami 2, and their expression was confirmed by western blot analysis. Enzyme-linked immunosorbent assay experiments indicated that these antibodies were able to specifically recognize 4-1BB without any cross-reactivity with other antigens. Flow cytometry analysis demonstrated an acceptable specific binding of the single chain variable fragments to 4-1BB expressed on CCRF-CEM cells, while no binding was observed with an irrelevant antibody. Anti-4-1BB single chain variable fragments enhanced surface CD69 expression and interleukin-2 production in stimulated CCRF-CEM cells which confirmed the agonistic effect of the selected single chain variable fragments. The data from this study have provided a rationale for further experiments involving the biological functions of anti-4-1BB single chain variable fragments in future studies.

scholarly journals Identification of Receptor Ligands by Screening Phage-Display Peptide LibrariesEx Vivoon Microdissected Kidney Tubules

2001 ◽  
Vol 12 (2) ◽  
pp. 308-316 ◽  
Author(s):  
ALEX ODERMATT ◽  
ANNETTE AUDIGÉ ◽  
CHRISTOPH FRICK ◽  
BRUNO VOGT ◽  
BRIGITTE M. FREY ◽  
...  
Keyword(s):  
Phage Display ◽  
Ex Vivo ◽  
Specific Binding ◽  
Cell System ◽  
Membrane Receptors ◽  
Direct Access ◽  
Kidney Tubules ◽  
Receptor Ligands ◽  
Renal Epithelial Cell ◽  
Linear Peptide

Abstract. A novel method to identify receptor ligands for defined renal tubular segments has been developed.Ex vivoscreening of phage-display peptide libraries on isolated intact rat proximal convoluted tubules (PCT) and cortical collecting ducts (CCD) allowed the direct access of phage to the basolateral surface of tubular epithelial cells. Two distinct peptide motifs were selected for CCD and PCT, indicating differential expression of some membrane receptors on the basolateral surface of defined kidney tubule segments. Using the linear peptide motif ELRGD(R/M)AX(W/L), recovered from freshly isolated rat CCD, mediated 16-fold selectivity of phage binding to CCD compared with PCT. Binding to CCD was 39-fold higher than that of a random control phage. Binding and subsequent internalization of phage, most likely by an integrin-mediated endocytosis pathway, was abolished by the addition of the corresponding synthetic peptide. Furthermore, the results demonstrate that presentation and flanking amino acids determine the specific binding properties of RGD ligands to their putative integrin receptors. The results emphasize the need of a native cell system for the identification of renal epithelial cell surface ligands. Such ligands are of potential relevance for the analysis of interactions between extracellular matrix and kidney tubules or for the development of improved vectors for kidney-specific drug delivery or gene transfer.

Screening of specific binding peptides using phage-display techniques and their biosensing applications

2021 ◽  
Vol 137 ◽  
pp. 116229
Author(s):  
Ping Xu ◽  
Subhadeep Ghosh ◽  
Anam Rana Gul ◽  
Jigna R. Bhamore ◽  
Jong Pil Park ◽  
...  
Keyword(s):  
Phage Display ◽  
Specific Binding ◽  
Binding Peptides

scholarly journals Isolation of isoform-specific binding proteins (Affimers) by phage display using negative selection

2017 ◽  
Vol 10 (505) ◽  
pp. eaan0868 ◽  
Author(s):  
Anna Ah-San Tang ◽  
Christian Tiede ◽  
David J. Hughes ◽  
Michael J. McPherson ◽  
Darren C. Tomlinson
Keyword(s):  
Phage Display ◽  
Negative Selection ◽  
Binding Proteins ◽  
Specific Binding

The development of a Glypican-3-specific binding peptide using in vivo and in vitro two-step phage display screening for the PET imaging of hepatocellular carcinoma

2020 ◽  
Vol 8 (20) ◽  
pp. 5656-5665
Author(s):  
Yushuang Qin ◽  
Siyuan Cheng ◽  
Yesen Li ◽  
Sijuan Zou ◽  
Minglong Chen ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Phage Display ◽  
Pet Imaging ◽  
Specific Binding ◽  
Normal Liver ◽  
Liver Uptake ◽  
Binding Peptide ◽  
Screening Approach

An in vivo and in vitro two-step phage display screening approach to identify Glypican-3 targeting peptides for the detection of hepatocellular carcinoma with low normal liver uptake.

scholarly journals Recognition of cell-specific binding of phage display derived peptides using an acoustic wave sensor

2002 ◽  
Vol 18 (6) ◽  
pp. 269-272 ◽  
Author(s):  
Alexandre M Samoylov ◽  
Tatiana I Samoylova ◽  
Mark G Hartell ◽  
Suram T Pathirana ◽  
Bruce F Smith ◽  
...  
Keyword(s):  
Acoustic Wave ◽  
Phage Display ◽  
Specific Binding ◽  
Acoustic Wave Sensor
Sign in / Sign up

Export Citation Format

Share Document