Sadia Tamanna ^*

• Chosun University, Gwangju, Republic of Korea

The creation of improved predictive models necessitates a thorough understanding of the molecular mechanisms behind AMPs' antibacterial activity. AMPs interact with membranes, causing perturbation, disrupting physiological events like cell wall biosynthesis or cell division, and/or translocating across membranes to target cytoplasmic components. Antibiotic resistance poses a significant threat to human health, prompting the investigation of new countermeasures. Antimicrobial peptides (AMPs), sourced both synthetically and naturally, exhibit broad-spectrum antimicrobial action with high specificity, resulting in minimal bacterial resistance. These peptides possess unique activities and structures, employing diverse mechanisms of action. This study explores the origins, structural characteristics, mechanisms, and context of AMPs' antibacterial and antibiofilm capabilities. AMPs kill bacteria by disrupting membranes or interfering with internal bacterial components. However, a gap remains in understanding the relationship between cytolytic activity across species and AMP structures due to the complex nature of their membrane interactions, which can alter AMP classes by mechanism. Various biophysical methods have been employed to study the impact of peptides and model membrane systems on cytolytic activity. A quantitative analysis of peptide binding to membranes and the resulting dynamic structural changes is crucial for characterizing this interaction. This study has reviewed findings that elucidate the multistep methods used by several AMPs in nature, potentially enhancing our ability to develop a new generation of effective antimicrobial treatments.