scholarly journals Corrigendum to “A Versatile Surface Bioengineering Strategy Based on Mussel-Inspired and Bioclickable Peptide Mimic”

Research ◽  
2021 ◽  
Vol 2021 ◽  
pp. 1-2
Author(s):  
Yu Xiao ◽  
Wenxuan Wang ◽  
Xiaohua Tian ◽  
Xing Tan ◽  
Tong Yang ◽  
...  
Keyword(s):  
Peptide Mimic

Polymerization-Defective Fibrinogen Variant γD364A Binds Knob “A” Peptide Mimic†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (33) ◽  
pp. 8607-8613 ◽  
Author(s):  
Sheryl R. Bowley ◽  
Betsy K. Merenbloom ◽  
Nobuo Okumura ◽  
Laurie Betts ◽  
Annie Heroux ◽  
...  
Keyword(s):  
Peptide Mimic

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.

scholarly journals Structural basis for the development of SARS 3CL protease inhibitors from a peptide mimic to an aza ‐decaline scaffold

Biopolymers ◽  
2016 ◽  
Vol 106 (4) ◽  
pp. 391-403 ◽  
Author(s):  
Kenta Teruya ◽  
Yasunao Hattori ◽  
Yasuhiro Shimamoto ◽  
Kazuya Kobayashi ◽  
Akira Sanjoh ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Structural Basis ◽  
Peptide Mimic ◽  
3Cl Protease

Human Immune Response to a Peptide Mimic ofNeisseria meningitidisSerogroup C in hu-PBMC-SCID Mice

Hybridoma ◽  
1999 ◽  
Vol 18 (2) ◽  
pp. 121-129 ◽  
Author(s):  
WENDY A. HUTCHINS ◽  
THOMAS KIEBER-EMMONS ◽  
GEORGE M. CARLONE ◽  
M.A. JULIE WESTERINK
Keyword(s):  
Immune Response ◽  
Scid Mice ◽  
Peptide Mimic ◽  
Human Immune Response ◽  
Human Immune

scholarly journals Identification of a peptide mimic of the L2/HNK-1 carbohydrate epitope

2002 ◽  
Vol 83 (6) ◽  
pp. 1380-1388 ◽  
Author(s):  
Maryline Simon-Haldi ◽  
Ned Mantei ◽  
Jens Franke ◽  
Hans Voshol ◽  
Melitta Schachner
Keyword(s):  
Carbohydrate Epitope ◽  
Peptide Mimic

scholarly journals A Stapled Peptide Mimic of the Pseudosubstrate Inhibitor PKI Inhibits Protein Kinase A

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1567 ◽  
Author(s):  
Jascha T. Manschwetus ◽  
George N. Bendzunas ◽  
Ameya J. Limaye ◽  
Matthias J. Knape ◽  
Friedrich W. Herberg ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Kinase Inhibitor ◽  
Stapled Peptide ◽  
Peptide Mimic ◽  
Cellular Environment ◽  
Ic50 Values ◽  
Dependent Protein ◽  
Peptide Targeting ◽  
Kinase A

Kinases regulate multiple and diverse signaling pathways and misregulation is implicated in a multitude of diseases. Although significant efforts have been put forth to develop kinase-specific inhibitors, specificity remains a challenge. As an alternative to catalytic inhibition, allosteric inhibitors can target areas on the surface of an enzyme, thereby providing additional target diversity. Using cAMP-dependent protein kinase A (PKA) as a model system, we sought to develop a hydrocarbon-stapled peptide targeting the pseudosubstrate domain of the kinase. A library of peptides was designed from a Protein Kinase Inhibitor (PKI), a naturally encoded protein that serves as a pseudosubstrate inhibitor for PKA. The binding properties of these peptide analogs were characterized by fluorescence polarization and surface plasmon resonance, and two compounds were identified with KD values in the 500–600 pM range. In kinase activity assays, both compounds demonstrated inhibition with 25–35 nM IC50 values. They were also found to permeate cells and localize within the cytoplasm and inhibited PKA activity within the cellular environment. To the best of our knowledge, these stapled peptide inhibitors represent some of the highest affinity binders reported to date for hydrocarbon stapled peptides.

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