Related Experiment Video
Updated: Jan 22, 2026

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
Published on: September 30, 2019
Panning using a phage-displayed random peptide library to identify peptides that antagonize the Helicobacter pylori
Yuxia Xiong1, Zhibang Yang1, Jin Zhang1
1Department of Pathogenic Biology, College of Basic Medical Sciences, Chongqing Medical University, Chongqing, 400016, China.
Abstract:
Helicobacter pylori is an important etiological factor involved in chronic gastritis, peptic ulcer, and gastric cancer. There are currently no optimal preventive or therapeutic interventions for H. pylori infection. H. pylori survives in the stomach by sensing and adapting to the highly acidic environment by using the two-component signal transduction system that contains the most widely known gastric acid receptor, ArsRS (which is composed of ArsS and ArsR). This study aimed to identify peptides that antagonize the acid-sensing domain of H. pylori ArsS. These peptides could be used to block the acid-sensing signal and thereby hinder H. pylori adaption to acidic environments to prevent its survival. Using proSite, the functional domains (including the N-terminal acid-sensing domain) of H. pylori J99 ArsS were predicted. The purified recombinant ArsS N-terminal acid-sensing protein (P-ArsS-A) was used as the target in a panning protocol in which peptides from the Ph.D.-7 Phage Display Peptide Library that could bind to P-ArsS-A were identified. As a result, eight phage clones that could specifically bind to P-ArsS-A were obtained and five amino acid sequences were identified, including P03 (MMSYPKH) and P06 (LTPMPNW). An in vitro minimum inhibitory concentration (MIC) evaluation showed that P03 and P06 significantly inhibited the growth of H. pylori J99. The MIC of P03 was 8 μM, and the MIC of P06 was >16 μM, indicating that P03 is a stronger inhibitor compared to P06. This was confirmed by colony counting on blood agar plates after P03 and P06 administration. Using homology modeling and molecular docking analysis, it was shown that P03 and P06 could bind to the ArsS N-terminal domain, and there were four shared binding sites: TYR25, ASN39, ARG73, and GLU74. Additionally, one hydrogen bond was found between P03 and ArsS, which is more cohesive than other forms of bonding (van der Waals force, other non-covalent bonds).
More Related Videos
07:53Peptides from Phage Display Library Modulate Gene Expression in Mesenchymal Cells and Potentiate Osteogenesis in Unicortical Bone Defects
Published on: December 10, 2010
12:55Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
Published on: January 17, 2015
Related Concept Videos
Peptide Bonds
Treating Helicobacter pylori in Peptic Ulcers: Antimicrobial Therapy
Peptide Identification Using Tandem Mass Spectrometry
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Agonism and Antagonism: Quantification
To quantify these effects, researchers use a dose-response curve, which provides valuable information about the potency and efficacy of a drug. Potency refers to...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Combined Effects of Drugs: Antagonism
The most common type is receptor antagonism, where one drug acts as an antagonist to block the effects of another drug by...