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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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Playback language: English
Abstract
*Clostridioides difficile* infections are a significant global health problem. This study focuses on developing peptide inhibitors to block Toxin A (*C. diff*). Using a combination of peptide binding design algorithms, molecular simulations, assays evaluating peptide-toxin binding, and surface plasmon resonance measurements, the researchers identified a peptide, SA1, that effectively blocks Toxin A in human colon epithelial cells. SA1 displays a K<sub>D</sub> of 56.1 ± 29.8 nM.
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
Tags
Clostridioides difficile
Toxin A
peptide inhibitors
human colon epithelial cells
binding affinity

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