Journal of Biosciences, 2018, vol 43, 4, pp. 707-715
Antibiotic resistance in bacteria is a major health concern. Antimicrobial peptides (AMPs) are a class of peptides that are efficient in killing most microbes yet development of resistance to AMPs is rare. However, complex secondary and tertiary structures and difficulties in isolating AMPs have limited their use as antibiotics. It has been demonstrated earlier that small peptides derived from human β defensin-3 (HBD-3) also show antibacterial activity. Here, we perform a detailed characterization of the antibacterial activity of one such derivative: CHRG01. While HBD-3 has 45 amino acids with three disulphide bonds and a β-sheet folded structure, CHRG01 has only 14 amino acids with the cysteine residues replaced by serine. The antibacterial nature of CHRG01 was studied using scanning electron microscopy (SEM), confocal microscopy, circular dichroism (CD) and small-angle X-ray scattering (SAXS). CD data show that CHRG01 is random coiled in solution. SEM and confocal studies show that the mode of action of CHRG01 is pore forming. SAXS studies show that CHRG01 induces a negative Gaussian curvature, the type of curvature needed for pore formation. The above results show that CHRG01, a small peptide without any complex structure, is capable of killing bacteria by permeabilizing their outer membranes.