Breaking disulfide bonds in a weakly bactericidal α-defensin unleashes a potent antimicrobial peptide with an altered conformation
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Harnessing antimicrobial peptides as bactericidal agents affords an attractive approach to developing new anti-infective therapies. We found that abolishing disulfide bonding in mouse cryptdin 1 (Crp1), a weakly bactericidal α-defensin of 35 residues, turned ... ...
