Home / Health & Beauty / MIT engineers repurpose wasp venom as an antibiotic drug that can kill bacteria but is nontoxic to human cells. In a study of mice, the peptide could completely eliminate Pseudomonas aeruginosa, a strain of bacteria that causes respiratory and other infections and is resistant to most antibiotics. : Health

MIT engineers repurpose wasp venom as an antibiotic drug that can kill bacteria but is nontoxic to human cells. In a study of mice, the peptide could completely eliminate Pseudomonas aeruginosa, a strain of bacteria that causes respiratory and other infections and is resistant to most antibiotics. : Health

The title of the post is a copy and paste from the title, subtitle and third paragraph of the linked academic press release here:

MIT engineers repurpose wasp venom as an antibiotic drug

Altered peptides from a South American wasp’s venom can kill bacteria but are nontoxic to human cells.

In a study of mice, the researchers found that their strongest peptide could completely eliminate Pseudomonas aeruginosa, a strain of bacteria that causes respiratory and other infections and is resistant to most antibiotics.

Journal Reference:

Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates

Marcelo D. T. Torres, Cibele N. Pedron, […]Cesar de la Fuente-Nunez

Communications Biology, volume 1, Article number: 221 (2018)

DOI: https://doi.org/10.1038/s42003-018-0224-2

Link: https://www.nature.com/articles/s42003-018-0224-2

Abstract

Antimicrobial peptides (AMPs) constitute promising alternatives to classical antibiotics for the treatment of drug-resistant infections, which are a rapidly emerging global health challenge. However, our understanding of the structure-function relationships of AMPs is limited, and we are just beginning to rationally engineer peptides in order to develop them as therapeutics. Here, we leverage a physicochemical-guided peptide design strategy to identify specific functional hotspots in the wasp-derived AMP polybia-CP and turn this toxic peptide into a viable antimicrobial. Helical fraction, hydrophobicity, and hydrophobic moment are identified as key structural and physicochemical determinants of antimicrobial activity, utilized in combination with rational engineering to generate synthetic AMPs with therapeutic activity in a mouse model. We demonstrate that, by tuning these physicochemical parameters, it is possible to design nontoxic synthetic peptides with enhanced sub-micromolar antimicrobial potency in vitro and anti-infective activity in vivo. We present a physicochemical-guided rational design strategy to generate peptide antibiotics.


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