<br/>The steep growth of antimicrobial resistance has resulted in focusing on Antimicrobial peptides (AMP) and the development of AMP mimicking agents to combat this nefarious issue. However lesser reports come up with adequate reasoning behind the driving force of the membrane perturbing nature. Here, the two branches of AMP mimics, peptoids and small molecules will be discussed along with the mode of action behind the antimicrobial properties displayed by the peptoids and small molecule mimics.<br/>To address this big challenge of mechanistic understanding, each of the compounds were introduced to the bacterial model membranes, and their interactions was recorded using solid state nuclear magnetic resonance spectroscopy. We observe that each of the mimics interact with the liposome as the global shape of the vesicles gets deformed. Also we observed a definite interaction with the fatty acyl chain as changes in order parameters were observed.<br/>To develop a thorough understanding of the pore forming abilities of these compounds, a fluorescent dye release studies was executed using both bacterial and mammalian model membranes. The calcein dye release test revealed that the small molecule mimics undergo a cooperative effect. For the peptoids investigated, the dye release could be correlated with their biological data.

Biophysical investigations of antimicrobial peptide mimics for mechanistic studies

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