scholarly journals Genetically-encoded discovery of proteolytically stable bicyclic inhibitors for morphogen NODAL

2021 ◽  
Author(s):  
Jeffrey Y.-K. Wong ◽  
Raja Mukherjee ◽  
Jiayuan Miao ◽  
Olena Bilyk ◽  
Vivian Triana ◽  
...  
Keyword(s):  
Peptide Libraries ◽  
Phage Library

A two-fold symmetric linchpin (TSL) converts readily available phage-displayed disulfide peptide libraries to proteolytically stable bicyclic peptides. The bicyclic phage library was screened to discover an antagonist of NODAL morphogen.

Latest Advances in OBOC Peptide Libraries. Improvements in Screening Strategies and Enlarging the Family From Linear to Cyclic Libraries

2016 ◽  
Vol 17 (5) ◽  
pp. 449-457 ◽  
Author(s):  
Maria C. Martínez-Ceron ◽  
Silvana L. Giudicessi ◽  
Soledad L. Saavedra ◽  
Juan M. Gurevich-Messina ◽  
Rosa Erra-Balsells ◽  
...  
Keyword(s):  
Peptide Libraries ◽  
Screening Strategies ◽  
The Family

Multiphosphorylated peptides: importance, synthetic strategies, and applications for studying biological mechanisms

2020 ◽  
Vol 18 (18) ◽  
pp. 3405-3422
Author(s):  
Mamidi Samarasimhareddy ◽  
Guy Mayer ◽  
Mattan Hurevich ◽  
Assaf Friedler
Keyword(s):  
Protein Function ◽  
Peptide Libraries ◽  
Biological Mechanisms

Advances in the synthesis of multiphosphorylated peptides and peptide libraries: tools for studying the effects of phosphorylation patterns on protein function and regulation.

scholarly journals Phage display demonstrates durable differences in serological profile by route of inoculation in primary infections of non-human primates with Dengue Virus 1

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jayant V. Rajan ◽  
Michael McCracken ◽  
Caleigh Mandel-Brehm ◽  
Greg Gromowski ◽  
Simon Pollett ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Phage Display ◽  
Denv Infection ◽  
Phage Library ◽  
Humoral Immune ◽  
Linear Peptide ◽  
Humoral Immune Responses ◽  
High Resolution Map ◽  
Domain Iii ◽  
Inoculation Route

AbstractNatural dengue virus (DENV) infections occur by mosquito bite but how the inoculation route affects the humoral immune response is unknown. We serologically profiled 20 non-human primates (NHP) from a prior study of DENV1 infection where animals were inoculated by mosquito (N = 10) or subcutaneous injection (N = 10). Using a comprehensive, densely tiled and highly redundant pan-flavivirus programmable phage library containing 91,562 overlapping 62 amino acid peptides, we produced a high-resolution map of linear peptide sequences enriched during DENV seroconversion. Profiles in mosquito-inoculated and subcutaneously-inoculated animals were similar up to 90 days after primary infection, but diverged at 1 year with differences in sero-reactivity in the Envelope (E; residues 215–406; p < 0.08), and Nonstructural-3 (NS3; residues 549–615; p < 0.05) proteins in mosquito-inoculated versus subcutaneously-inoculated animals. Within the E protein, residues 339–384 in domain III accounted for > 99% of the observed sero-reactivity difference. Antibody breadth did not vary by mode of inoculation. The differential reactivity to E domain III seen by phage display validated orthogonally by ELISA, but did not correlate with late neutralization titers. Serological profiling of humoral immune responses to DENV infection in NHP by programmable phage display demonstrated durable differences in sero-reactivity by route of inoculation.

scholarly journals Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries.

1994 ◽  
Vol 269 (39) ◽  
pp. 23853-23856
Author(s):  
A.B. Sparks ◽  
L.A. Quilliam ◽  
J.M. Thorn ◽  
C.J. Der ◽  
B.K. Kay
Keyword(s):  
Peptide Libraries ◽  
Random Peptide ◽  
Random Peptide Libraries ◽  
Identification And Characterization

scholarly journals Isolation and characterizations of a novel recombinant scFv antibody against exotoxin A of Pseudomonas aeruginosa

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Zahra Shadman ◽  
Safar Farajnia ◽  
Mohammad Pazhang ◽  
Mohammadreza Tohidkia ◽  
Leila Rahbarnia ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Virulence Factors ◽  
High Reactivity ◽  
Scfv Antibody ◽  
Phage Library ◽  
Human Antibody ◽  
Exotoxin A ◽  
Phage Elisa ◽  
Human Scfv ◽  
Domain I

Abstract Background Pseudomonas aeruginosa is the leading cause of nosocomial infections, especially in people with a compromised immune system. Targeting virulence factors by neutralizing antibodies is a novel paradigm for the treatment of antibiotic-resistant pseudomonas infections. In this respect, exotoxin A is one of the most potent virulence factors in P. aeruginosa. The present study was carried out to identify a novel human scFv antibody against the P. aeruginosa exotoxin A domain I (ExoA-DI) from a human scFv phage library. Methods The recombinant ExoA-DI of P. aeruginosa was expressed in E. coli, purified by Ni-NTA column, and used for screening of human antibody phage library. A novel screening procedure was conducted to prevent the elimination of rare specific clones. The phage clone with high reactivity was evaluated by ELISA and western blot. Results Based on the results of polyclonal phage ELISA, the fifth round of biopanning leads to the isolation of several ExoA-DI reactive clones. One positive clone with high affinity was selected by monoclonal phage ELISA and used for antibody expression. The purified scFv showed high reactivity with the recombinant domain I and full-length native exotoxin A. Conclusions The purified anti-exotoxin A scFv displayed high specificity against exotoxin A. The human scFv identified in this study could be the groundwork for developing a novel therapeutic agent to control P. aeruginosa infections.

scholarly journals Phage-Display Based Discovery and Characterization of Peptide Ligands against WDR5

Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1225
Author(s):  
Jiawen Cao ◽  
Tiantian Fan ◽  
Yanlian Li ◽  
Zhiyan Du ◽  
Lin Chen ◽  
...  
Keyword(s):  
Phage Display ◽  
Cyclic Peptide ◽  
Protein Complexes ◽  
Peptide Ligands ◽  
Phage Library ◽  
Cancer Drug ◽  
Protein Protein Interaction ◽  
Phage Display Technique ◽  
Peptide Mimic ◽  
Human Proteins

WD40 is a ubiquitous domain presented in at least 361 human proteins and acts as scaffold to form protein complexes. Among them, WDR5 protein is an important mediator in several protein complexes to exert its functions in histone modification and chromatin remodeling. Therefore, it was considered as a promising epigenetic target involving in anti-cancer drug development. In view of the protein–protein interaction nature of WDR5, we initialized a campaign to discover new peptide-mimic inhibitors of WDR5. In current study, we utilized the phage display technique and screened with a disulfide-based cyclic peptide phage library. Five rounds of biopanning were performed and isolated clones were sequenced. By analyzing the sequences, total five peptides were synthesized for binding assay. The four peptides are shown to have the moderate binding affinity. Finally, the detailed binding interactions were revealed by solving a WDR5-peptide cocrystal structure.

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