AI Article Synopsis
- - Three encrypted peptides from human apolipoprotein B were found to have strong antimicrobial effects against drug-resistant bacteria in animal studies.
- - These peptides work by disrupting bacterial membranes, preventing biofilm formation, and reducing inflammation, while also increasing the effectiveness of traditional antibiotics without promoting resistance.
- - A modified version of one peptide was created to resist breakdown by enzymes and showed promise in fighting infections in mice, suggesting that human blood could be a valuable source for new antibiotics.
Article Abstract
Encrypted peptides have been recently found in the human proteome and represent a potential class of antibiotics. Here we report three peptides derived from the human apolipoprotein B (residues 887-922) that exhibited potent antimicrobial activity against drug-resistant , , and both and in an animal model. The peptides had excellent cytotoxicity profiles, targeted bacteria by depolarizing and permeabilizing their cytoplasmic membrane, inhibited biofilms, and displayed anti-inflammatory properties. Importantly, the peptides, when used in combination, potentiated the activity of conventional antibiotics against bacteria and did not select for bacterial resistance. To ensure translatability of these molecules, a protease resistant retro-inverso variant of the lead encrypted peptide was synthesized and demonstrated anti-infective activity in a preclinical mouse model. Our results provide a link between human plasma and innate immunity and point to the blood as a source of much-needed antimicrobials.
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| http://dx.doi.org/10.1021/acsnano.1c04496 | DOI Listing |
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