Atomic force spectroscopy with magainin 1 functionalized tips and biomimetic supported lipid membranes

Antimicrobial peptides are molecules synthesized by living organisms as the first line of defense against bacteria, fungi, parasites, or viruses. Since their biological activity is based on destabilization of the microbial membranes, a study of direct interaction forces between antimicrobial peptides and biomimetic membranes is very important for understanding the molecular mechanisms of their action. Herein, we use atomic force spectroscopy to probe the interaction between atomic force microscopy (AFM) tips functionalized with magainin 1 and supported lipid bilayers (SLBs) mimicking electrically uncharged membranes of normal eukaryotic cells and negatively charged membranes of bacterial cells. The investigations performed on negatively charged SLBs showed that the magainin 1 functionalized AFM tips are quickly adsorbed into the SLBs when they approach, while they adhere strongly to the lipid membrane when retracted. On contrary, same investigations performed on neutral SLBs showed mechanical resistance of the lipid membrane to the tip breakthrough and negligible adhesion force at detachment.

Automated summary

This study investigates the interaction between antimicrobial peptides and biomimetic membranes using atomic force microscopy. The results show that negatively charged membranes have a stronger adsorption capacity for the peptides, while neutral membranes exhibit mechanical resistance to peptide penetration.