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Fig. 4 | Irish Veterinary Journal

Fig. 4

From: Confronting the complexities of antimicrobial management for Staphylococcus aureus causing bovine mastitis: an innovative paradigm

Fig. 4

Structure of antimicrobial peptide (AMPs): A β-sheet, B Linear, C α-helical, and D combined structure. The figure was created using UCSF Chimera (http://www.cgl.ucsf.edu/chimera) The mechanisms underlining the AMPs antimicrobial proprieties is believed to be due to cell membrane disruptions. There is four mechanisms for AMPs membrane distribution has been identified including “Barrel stave”, “toroidal pore”, “carpet”, and ‘’aggregate’’ as describing in our previous study [62] (Fig. 5). Besides the damaging membranes, AMPs can kill bacteria by targeting and inhibiting the biosynthesis of proteins, nucleic acids, and essential enzymes required and involved in vital biological pathways and ultimately lead to cell lysis. The mechanisms for intracellular AMPs are summarized in Fig. 6. The antimicrobial activity of AMPs is particularly linked with its corresponding amino acid composition and physicochemical characteristics [81]. In addition to their direct antimicrobial activity, AMPs possess immunomodulatory properties, which stimulate the immune reaction of the host animal. By stimulating the functioning of immune cells and enhancing their functionality, AMPs contribute to a higher and effective protection against bacterial invaders [84, 86]. In an era of increasing antibiotic resistance, AMPs are emerging as a potent and promising therapeutic alternative. The AMP study demonstrates a remarkable advancement in the development of simple and accountable solutions in the prevention of S. aureus associated mastitis in dairy cattle [83,84,85]

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