1.D.107.  The Putative Broad-spectrum Antimicrobial Peptide, HJH-1 (HJH-1) Family  

Wang et al. 2018 examined the antimicrobial and membrane activity of HJH-1, a cationic peptide derived from the hemoglobin alpha-subunit of bovine erythrocytes P3. HJH-1 showed potent antimicrobial activity against different bacterial species associated with infection and causes weaker hemolysis of erythrocytes, at least five times the minimal inhibitory concentration (MIC). HJH-1 is stabile in a range of temperatures, pH values, and ionic strength. In the presence of HJH-1 (1x MIC), Escherichia coli membranes rapidly depolarised although red blood cells showed gradual hyperpolarisation. Scanning electron microscopy and transmission electron micrographs showed that HJH-1 (1x MIC) damaged the membranes of Escherichia coli, Staphylococcus aureus, and Candida albicans. Thus, HJH-1 has broad-spectrum antimicrobial activity by disrupting microbial membranes (Wang et al. 2018).



Wang, Q., Y. Xu, M. Dong, B. Hang, Y. Sun, L. Wang, Y. Wang, J. Hu, and W. Zhang. (2018). HJH-1, a Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity Antimicrobial Peptide. Molecules 23:.