For some peptides, killing bacteria is an internal job

Peptides can be used to solve the thorny problem of human antibiotic resistance

The Rice laboratory of chemist Anatoly Kolomeisky simulated a series of antimicrobial peptides (AMPs) that help natural and diverse molecules in biological systems to evaluate the mechanisms they use to stop harmful bacteria

amp kills bacteria in two steps: first attaches to the cell membrane of the bacteria, and then inhibits the bacteria

According to their calculations, the invasion seems to depend on a large number of peptides-even millions of peptides-entering the bacteria, but the peptides needed to inhibit the bacteria from the inside may be much less, because the bacteria are particularly good at sticking gears inside

"AMP can inhibit bacteria in many ways," said Kolomeiski, a professor of chemistry

The research was published in "Interface.

Understanding the mechanism of peptides requires the establishment of a theoretical framework to test the speed at which different AMP populations can remove bacteria from the system

The results are consistent with the experimental data and help explain how and why amps show effectiveness in a wide range of concentrations

With the presence of more types of amps, peptides are better at entering and dividing cells

Teimouri said: "The high heterogeneity of the absorbed amp amount corresponds to the fast-entering peptides, while the low heterogeneity describes the fast-killing peptides

The researchers hope that their model can help others design therapeutic antimicrobial peptides that succeed where antibiotics fail, especially by adjusting their ability to enter the target bacteria

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DOI

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Single-cell stochastic modelling of the action of antimicrobial peptides on bacteria