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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).

References associated with 1.D.107 family:

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:. 30110916