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000475051 1001_ $$0P:(DE-HGF)0$$aEngelberg, Yizhaq$$b0
000475051 245__ $$aRare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides
000475051 260__ $$aColumbus, Ohio$$bAmerican Chemical Soc.$$c2022
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000475051 520__ $$aHuman LL-37$_{17–29}$ is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-37$_{17–29}$ bearing an I24C substitution of most buried position in the fibril revealed disulfide-bonded dimers that further assembled into a fibrillar structure of densely packed helices. We further demonstrated the position-dependent controllable antibacterial activity of LL-37$_{17–29}$ I24C and other cysteine mutants, mediated by regulation of intermolecular disulfide bonds and their role in the formation of supramolecular structures. The morphology of the fibrils and their antibacterial mechanism of action might be dependent on their interactions with specific bacteria. The significant effect of disulfide bonds on the assembly into supramolecular structures and their sensitivity to reducing/oxidizing conditions may explain why short helical antimicrobial peptides with a single cysteine and an odd number of cysteines are selected against in nature.
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000475051 7001_ $$0P:(DE-HGF)0$$aRagonis-Bachar, Peleg$$b1
000475051 7001_ $$0P:(DE-H253)PIP1026961$$aLandau, Meytal$$b2$$eCorresponding author
000475051 773__ $$0PERI:(DE-600)2006291-6$$a10.1021/acs.biomac.1c01353$$gp. acs.biomac.1c01353$$n3$$p926 – 936$$tBiomacromolecules$$v23$$x1525-7797$$y2022
000475051 8564_ $$uhttps://pubs.acs.org/doi/abs/10.1021/acs.biomac.1c01353
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