We demonstrate that retrocyclins (RCs), promising therapeutic peptides, neutralize bacterial toxins by inducing their unfolding and exposing hydrophobic regions, normally buried in the molecule interior, to solvents. RC-induced toxin unfolding leads to toxin precipitation, proneness to proteolytic degradation and abrogated activity.

Keywords:
bacterial toxins, defensins, retrocyclins, structural plasticity, thermodynamic instability, unfolding
© The Authors Journal compilation © 2015 Biochemical Society
2015
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