Identification of peptidyl mimics of bioactive gibberellin recognized by an antibody.

Biosci Biotechnol Biochem

Department of Applied Biological Chemistry, University of Tokyo, Japan.

Published: November 2004

We screened a phage display peptide library for peptidyl mimotopes of gibberellin against anti-bioactive gibberellin antibody. The peptides obtained were grouped into two homologous sequences and their binding to the antibody was put in competition with free GA(4) but not with GA(4) methylester, suggesting that the peptides behave as mimics of GA(4). As an application, the phage display peptide was shown to work as a tracer for enzyme-linked immunosorbent assay (ELISA) analysis of GA(4).

Download full-text PDF

Source
http://dx.doi.org/10.1271/bbb.68.2408DOI Listing

Publication Analysis

Top Keywords

phage display
8
display peptide
8
identification peptidyl
4
peptidyl mimics
4
mimics bioactive
4
bioactive gibberellin
4
gibberellin recognized
4
recognized antibody
4
antibody screened
4
screened phage
4

Similar Publications

Background/objectives: Anterior Gradient-2 (AGR2/PDIA17) is a member of the protein disulfide isomerase (PDI) family of oxidoreductases. AGR2 is up-regulated in several solid tumors, including pancreatic ductal adenocarcinoma (PDAC). Given the dire need for new therapeutic options for PDAC patients, we investigated the expression and function of AGR2 in PDAC and developed a novel series of affinity-matured AGR2-specific single-chain variable fragments (scFvs) and monoclonal antibodies.

View Article and Find Full Text PDF

Antibodies and antibody mimics are extensively used in the pharmaceutical industry, where stringent safety standards are required. Implementing heat sterilization during or after the manufacturing process could help prevent contamination by viruses and bacteria. However, conventional antibodies and antibody mimics are not suitable for heat sterilization because they irreversibly denature at high temperatures.

View Article and Find Full Text PDF

Mechanistic Analysis of Peptide Affinity to Single-Walled Carbon Nanotubes and Volatile Organic Compounds Using Chemiresistors.

ACS Appl Mater Interfaces

December 2024

Air Force Research Laboratory, 711th Human Performance Wing, Wright-Patterson Air Force Base, Wright-Patterson AFB, Ohio 45433, United States.

Peptides, due to their diverse and controllable properties, are used as both liquid and gas phase recognition elements for both biological and chemical targets. While it is well understood how binding of a peptide to a biomolecule can be converted into a sensing event, there is not the same mechanistic level of understanding with regard to how peptides modulate the selectivity of semiconductor/conductor-based gas sensors. Notably, a rational, mechanistic study has not yet been performed to correlate peptide properties to the sensor response for volatile organic compounds (VOCs) as a function of chemical properties.

View Article and Find Full Text PDF

Biologically produced protein drugs are generally susceptible to degradation by proteases and often exhibit immunogenicity. To address this issue, mirror-image peptide/protein binders consisting of D-amino acids have been developed so far through the mirror-image phage display technique. Here, we develop a mirror-image protein binder derived from a monobody, one of the promising protein scaffolds, utilizing two notable technologies: chemical protein synthesis and TRAP display, an improved version of mRNA display.

View Article and Find Full Text PDF

Mirror-image proteins, composed of D-amino acids, are an attractive therapeutic modality, as they exhibit high metabolic stability and lack immunogenicity. Development of mirror-image binding proteins is achieved through chemical synthesis of D-target proteins, phage display library selection of L-binders and chemical synthesis of (mirror-image) D-binders that consequently bind the physiological L-targets. Monobodies are well-established synthetic (L-)binding proteins and their small size (~90 residues) and lack of endogenous cysteine residues make them particularly accessible to chemical synthesis.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!