AI Article Synopsis
- Clostridioides difficile infections are common and target the large intestine, primarily through two exotoxins, A and B.
- Researchers are exploring short peptides that can inhibit these toxins as a treatment strategy.
- The study successfully developed a peptide, SA1, which effectively blocks Toxin A's toxicity in human colon cells, showing strong binding affinity as measured by surface plasmon resonance.
Article Abstract
Infections by Clostridioides difficile, a bacterium that targets the large intestine (colon), impact a large number of people worldwide. Bacterial colonization is mediated by two exotoxins: toxins A and B. Short peptides that can be delivered to the gut and inhibit the biocatalytic activity of these toxins represent a promising therapeutic strategy to prevent and treat C. diff. infection. We describe an approach that combines a Peptide Binding Design (PepBD) algorithm, molecular-level simulations, a rapid screening assay to evaluate peptide:toxin binding, a primary human cell-based assay, and surface plasmon resonance (SPR) measurements to develop peptide inhibitors that block Toxin A in colon epithelial cells. One peptide, SA1, is found to block TcdA toxicity in primary-derived human colon (large intestinal) epithelial cells. SA1 binds TcdA with a K of 56.1 ± 29.8 nM as measured by surface plasmon resonance (SPR).
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10460389 | PMC |
| http://dx.doi.org/10.1038/s42003-023-05242-x | DOI Listing |
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