Specificity of Interaction of Antimicrobial Peptide with Cell Membrane

<p>Antimicrobial resistance (AMR) is an increasing global health threat due to its rising incidence worldwide. Resistant microbial infections have become difficult to treat and pose serious risks to patients. In 2019, AMR was responsible for approximately 1.27 million deaths globally, with numbers continuing to rise. The World Health Organization (WHO) has highlighted the urgent need for new antibiotics with novel mechanisms of action and low toxicity to combat this issue. Antimicrobial peptides (AMPs) represent a promising solution. These peptides exhibit broad-spectrum antimicrobial activity and rapid killing kinetics, reducing the likelihood of resistance development. AMPs primarily target bacterial cell membranes. Their hydrophobic side chains contribute both to membrane interaction and to peptide stability. This study investigates the interactions of a series of small AMPs with liposomes mimicking bacterial membranes (DOPC/DOPG, 7:3 molar ratio) and mammalian membranes (DOPC/cholesterol, 9:1 molar ratio). Samples at different peptide-to-lipid molar ratios (1:20 to 1:2 molar ratio) were analyzed using 1H and 31P nuclear magnetic resonance (NMR) spectroscopy. Changes in 1H and 31P spectral signals indicated (1) varied modes of peptide association with liposomes and (2) alterations in lipid bilayer integrity. Further, investigations will explore AMP interactions with membrane mimics using complementary techniques such as surface plasmon resonance and fluorescence quenching, alongside NMR spectroscopy.</p>

Name thesis:degree_name

Master of Science (MS)

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Pharmaceutical Sciences

Year

2025

Author dc:creator

• Kumar Jha, Srishhti

Contributors dc:contributor

• Innokentiy Maslennikov
• Keykavous Parang
• Sherif Elshahawi

• Antimicrobial Peptide
• Cytotoxicity
• AMR
• NMR
• Tryptophan
• Other Pharmacy and Pharmaceutical Sciences

Repository record dc:identifier

https://digitalcommons.chapman.edu/pharmaceutical_sciences_theses/40

OAI identifier oai:identifier

oai:digitalcommons.chapman.edu:pharmaceutical_sciences_theses-1041