Antibacterial protein 3

The photoreductive synthesis and antibacterial activity of silver nanoparticles (AgNP) prepared in the presence of bovine serum albumin (BSA) and lysozyme (LZ) were evaluated. AgNP@BSA showed similar antibacterial activity to those stabilized with citrate (AgNP@CIT) and to an AgNO3 solution, suggesting the releases of Ag+ as the mechanism of death. In contrast, AgNP@LZ solutions showed no activity, although LZ behaves as a moderately antibacterial peptide. Furthermore, the addition of LZ to the AgNP@CIT or AgNP@BSA solutions induced their agglomeration and suppressed their original antibacterial efficacy. This antagonistic antibacterial effect exerted by LZ on AgNPs is associated with electrostatic interactions exerted by LZ. Specific metal-LZ interactions produce a harder protein corona on AgNP@LZ that retains Ag+, while LZ acts as a glue for AgNP@CIT or AgNP@LZ due to its opposite electrical charge, besides strong binding to Ag+avoiding the bactericide effect. Therefore, bactericidal effects of AgNP in biological media may be modulated by specific protein interactions.

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.

Soy protein isolate (SPI) is green, high-yield natural plant protein, which is widely applied in industry (packing material and adhesives) and tissue engineering. It is meaningful to improve the antibacterial property of soy protein isolate to fabricate versatile safe products to meet people's requirements. In this study, quaternized soy protein isolate (QSPI) was synthesized by the reaction between 2,3-epoxypropyltrimethylammonium chloride (EPTMAC) and SPI. The positive charged (17.8 ± 0.23 mV) quaternary ammonium groups endow the QSPI with superior antibacterial properties against multiple bacteria in vitro and in vivo. Notably, QSPI maintains its good biocompatibility and promotes bacterial-infected wound healing in rat models. Furthermore, QSPI possesses superior water solubility in a broad pH range than raw SPI. Altogether, this soy protein isolate derivative with antibacterial property and superior water solubility may extend the application of SPI in industry and tissue engineering.