Nature’s design principles for antimicrobial peptides (AMPs)

Many antimicrobial peptides in our immune system kill bacteria by punching holes in their membranes. Scientists have been researching antimicrobial peptides for more than 30 years, and there is currently a large effort to mimic their antimicrobial action in order to fight antibiotic-resistant bacteria and emerging pathogens. A research team from the Gerard Wong group at UCLA Bioengineering has discovered an important pattern in the amino acid content of antimicrobial peptides and has shown that it is consistent with all 1,080 known peptides in the antimicrobial database. Nathan Schmidt is the lead author of this work, which was published in the Journal of the American Chemical Society. Details are in the following press release.

Link to PDF file on website: Schmidt 2011 JACS

Link to news coverage: UCLA

Four different types of membrane destabilization mechanisms: pore formation, blebbing, budding, and vesicularization. All four of these mechanisms require negative Gaussian curvature in the target membrane (also known as ‘saddle-splay’ deformations, the type of curvature found on the inside of a donut hole, which is covered with curved patches shaped like Pringles potato chips). This requirement places constraints on the amino acid content of AMPs, which controls the proportion of lysines, arginines, and hydrophobic residues.

Four different types of membrane destabilization mechanisms: pore formation, blebbing, budding, and vesicularization. All four of these mechanisms require negative Gaussian curvature in the target membrane (also known as ‘saddle-splay’ deformations, the type of curvature found on the inside of a donut hole, which is covered with curved patches shaped like Pringles potato chips). This requirement places constraints on the amino acid content of AMPs, which controls the proportion of lysines, arginines, and hydrophobic residues.

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