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Design of 8-mer peptides that block *Clostridioides difficile* toxin A in intestinal cells

Medicine and Health

Design of 8-mer peptides that block *Clostridioides difficile* toxin A in intestinal cells

S. Sarma, C. M. Catella, et al.

Discover groundbreaking research conducted by Sudeep Sarma, Carly M. Catella, and their team, focusing on peptide inhibitors that effectively block Toxin A of *Clostridioides difficile* in human colon epithelial cells. Their identified peptide, SA1, shows promising binding affinity, opening avenues for innovative treatments against a pressing global health issue.

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~3 min • Beginner • English
Abstract
Infections by Clostridioides difficile, a bacterium that targets the large intestine, are mediated by two exotoxins, toxins A and B. Short peptides that can be delivered to the gut and inhibit the catalytic activity of these toxins represent a promising therapeutic strategy. This study combines a Peptide Binding Design (PepBD) algorithm, molecular simulations, a rapid bead-based assay for peptide:toxin binding, a primary human colon epithelial cell assay, and surface plasmon resonance (SPR) measurements to develop peptide inhibitors that block Toxin A in intestinal epithelial cells. One peptide, SA1, blocks TcdA toxicity in primary-derived human colon epithelial cells and binds TcdA with a KD of 56.1 ± 29.8 nM by SPR.
Publisher
Communications Biology
Published On
Aug 26, 2023
Authors
Sudeep Sarma, Carly M. Catella, Ellyce T. San Pedro, Xingqing Xiao, Deniz Durmusoglu, Stefano Menegatti, Nathan Crook, Scott T. Magness, Carol K. Hall
DOI
https://doi.org/10.1038/s42003-023-05242-x
Tags
Clostridioides difficile
Toxin A
peptide inhibitors
human colon epithelial cells
binding affinity

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