HJH-1, a Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity Antimicrobial Peptide.

Qing Wang,Jianhe Hu,Mengmeng Dong,Yawei Sun,Bolin Hang,Wenju Zhang,Yongqiang Wang,Yanzhao Xu,Lei Wang

doi:10.3390/molecules23082026

Abstract

With the overuse of antibiotics, multidrug-resistant bacteria pose a significant threat to human health. Antimicrobial peptides (AMPs) are a promising alternative to conventional antibiotics. This study examines the antimicrobial and membrane activity of HJH-1, a cationic peptide derived from the hemoglobin α-subunit of bovine erythrocytes P3. HJH-1 shows potent antimicrobial activity against different bacterial species associated with infection and causes weaker hemolysis of erythrocytes, at least five times the minimum inhibitory concentration (MIC). HJH-1 has good stability to tolerance temperature, pH value, and ionic strength. The anionic membrane potential probe bis-(1,3-dibutylbarbituric acid) trimethine oxonol [DiBAC4(3)] and propidium iodide are used as indicators of membrane integrity. In the presence of HJH-1 (1× MIC), Escherichia coli membranes rapidly depolarise, whereas red blood cells show gradual hyperpolarisation. Scanning electron microscopy and transmission electron micrographs show that HJH-1 (1× MIC) damaged the membranes of Escherichia coli, Staphylococcus aureus, and Candida albicans. In conclusion, HJH-1 damages the integrity of the bacterial membrane, preventing the growth of bacteria. HJH-1 has broad-spectrum antibacterial activity, and these activities are performed by changing the normal cell transmembrane potential and disrupting the integrity of the bacterial membrane.

Highlights

The emergence of antibiotic-resistant strains of bacteria is a serious threat to public health, such as the appearance of bacteria with New Delhi metallo-β-lactamase (NDM-1) [1,2]
Our team isolated P3 from the hemoglobin α-subunit of bovine erythrocytes [15], and this study examines the antibacterial activity of P3 analogue HJH-1
HJH-1 was synthesized to 95% purity as indicated by reverse phase higher performance liquid chromatography (RP-HPLC) purity (Figure 1A)

Summary

Introduction

The emergence of antibiotic-resistant strains of bacteria is a serious threat to public health, such as the appearance of bacteria with New Delhi metallo-β-lactamase (NDM-1) [1,2]. Such bacteria are spreading in communities throughout the world. Traditional antibiotics kill bacteria by disturbing or blocking their normal metabolic processes. By modifying their genetic structure and the antibiotic target site, bacteria can avoid or resist antibiotics. There is an urgent need to develop innovative therapies to treat infections caused by multidrug-resistant bacteria. With their distinct mechanism of action against a spectrum of bacteria and viruses, including multidrug-resistant bacteria and human immunodeficiency virus (HIV) [5], antimicrobial peptides (AMPs) are potential important therapeutic agents [6]

Methods

Results

Discussion

Conclusion