Generation of inhibitory peptides for IKKε from a kinase‐focused phage library of helix‐loop‐helix peptides

2021 ◽  
Author(s):  
Kousuke Mihara ◽  
Natsumi Nakajima ◽  
Ikuo Fujii ◽  
Daisuke Fujiwara
Keyword(s):  
Phage Library ◽  
Inhibitory Peptides ◽  
Helix Loop Helix

Selection of inhibitory peptides for Aurora-A kinase from a phage-displayed library of helix–loop–helix peptides

2010 ◽  
Vol 20 (5) ◽  
pp. 1776-1778 ◽  
Author(s):  
Daisuke Fujiwara ◽  
Zhengmao Ye ◽  
Masaki Gouda ◽  
Koichi Yokota ◽  
Takeshi Tsumuraya ◽  
...  
Keyword(s):  
Aurora A Kinase ◽  
Aurora A ◽  
Inhibitory Peptides ◽  
Helix Loop Helix ◽  
Selection Of

Screening of ACE-inhibitory peptides from a random peptide-displayed phage library using ACE-coupled liposomes

2007 ◽  
Vol 131 (2) ◽  
pp. 144-149 ◽  
Author(s):  
Yoichi Kumada ◽  
Naoya Hashimoto ◽  
Fida Hasan ◽  
Masaaki Terashima ◽  
Kazuhiro Nakanishi ◽  
...  
Keyword(s):  
Phage Library ◽  
Random Peptide ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Dihydrofolate reductase inhibitory peptides screened from a structured designed β-loop peptide library displayed on phage

2015 ◽  
Vol 11 (10) ◽  
pp. 2713-2716 ◽  
Author(s):  
Hiroshi Tsutsumi ◽  
Kazuhiko Nakano ◽  
Hisakazu Mihara
Keyword(s):  
Dihydrofolate Reductase ◽  
Peptide Library ◽  
Phage Library ◽  
Loop Structure ◽  
Inhibitory Peptides ◽  
Β Sheet

Enzyme inhibitory peptides with a loop structure stabilized using an antiparallel β-sheet scaffold (β-loop peptide) were obtained from a designed peptide phage library.

Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong
Keyword(s):  
Snake Venom ◽  
Protein Families ◽  
Traditional Medicines ◽  
Phospholipases A2 ◽  
Inhibitory Peptides ◽  
Sds Page ◽  
Deinagkistrodon Acutus ◽  
Venom Proteins ◽  
Proteins And Peptides

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.

Identification of ecto-PKC on surface of human platelets: role in maintenance of latent fibrinogen receptors

2000 ◽  
Vol 278 (6) ◽  
pp. H2008-H2019 ◽  
Author(s):  
Anna Babinska ◽  
Michael V. Hogan ◽  
Tomasz Sobocki ◽  
Malgorzata B. Sobocka ◽  
Yigal H. Ehrlich ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Calcium Concentration ◽  
Surface Protein ◽  
Human Platelets ◽  
Surface Proteins ◽  
Free Calcium ◽  
Platelet Surface ◽  
Inhibitory Peptides ◽  
Intracellular Free Calcium Concentration ◽  
Free Calcium Concentration

Human platelets express a protein phosphorylation system on their surface. A specific protein kinase C (PKC) antibody, monoclonal antibody (MAb) 1.9, which binds to the catalytic domain of PKC and inhibits its activity, causes the aggregation of intact platelets while inhibiting the phosphorylation of platelet surface proteins. Photoaffinity labeling with 100 nM 8-azido-[α32P]ATP identified this ecto-PKC as a single surface protein of 43 kDa sensitive to proteolysis by extracellular 0.0005% trypsin. Inhibition of the binding of 8-azido-[α32P]ATP to the 43-kDa surface protein by MAb 1.9 identified this site as the active domain of ecto-PKC. Covalent binding of the azido-ATP molecule to the 43-kDa surface protein inhibited the phosphorylative activity of the platelet ecto-PKC. Furthermore, PKC pseudosubstrate inhibitory peptides directly induced the aggregation of platelets and inhibited azido-ATP binding to the 43-kDa protein. Platelet aggregation induced by MAb 1.9 and by PKC inhibitory peptides required the presence of fibrinogen and resulted in an increase in the level of intracellular free calcium concentration. This increase in intracellular free calcium concentration induced by MAb 1.9 was found to be dependent on the binding of fibrinogen to activated GPIIb/IIIa integrins, suggesting that MAb 1.9 causes Ca2+flux through the fibrinogen receptor complex. We conclude that a decrease in the state of phosphorylation of platelet surface proteins caused by inhibition of ecto-PKC results in membrane rearrangements that can induce the activation of latent fibrinogen receptors, leading to platelet aggregation. Accordingly, the maintenance of a physiological steady state of phosphorylation of proteins on the platelet surface by ecto-PKC activity appears to be one of the homeostatic mechanisms that maintain fibrinogen receptors of circulating platelets in a latent state that cannot bind fibrinogen.

scholarly journals Isolation and Characterization Of Rice R Genes: Evidence for Distinct Evolutionary Paths in Rice and Maize

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 1021-1031 ◽  
Author(s):  
Jianping Hu ◽  
Beth Anderson ◽  
Susan R Wessler
Keyword(s):  
Gene Family ◽  
Gene Families ◽  
Chromosome 1 ◽  
R Gene ◽  
R Genes ◽  
Helix Loop Helix ◽  
Isolation And Characterization ◽  
Undetermined Function ◽  
Evolutionary Paths

Abstract R and B genes and their homologues encode basic helix-loop-helix (bHLH) transcriptional activators that regulate the anthocyanin biosynthetic pathway in flowering plants. In maize, R/B genes comprise a very small gene family whose organization reflects the unique evolutionary history and genome architecture of maize. To know whether the organization of the R gene family could provide information about the origins of the distantly related grass rice, we characterized members of the R gene family from rice Oryza sativa. Despite being a true diploid, O. sativa has at least two R genes. An active homologue (Ra) with extensive homology with other R genes is located at a position on chromosome 4 previously shown to be in synteny with regions of maize chromosomes 2 and 10 that contain the B and R loci, respectively. A second rice R gene (Rb) of undetermined function was identified on chromosome 1 and found to be present only in rice species with AA genomes. All non-AA species have but one R gene that is Ra-like. These data suggest that the common ancestor shared by maize and rice had a single R gene and that the small R gene families of grasses have arisen recently and independently.

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