Journal Article

PUBDB-2022-01162

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides

Engelberg, Y. ; Ragonis-Bachar, P. ; Landau, M. (Corresponding author)CSSB*EMBL*

2022
American Chemical Soc. Columbus, Ohio

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Please use a persistent id in citations: doi:10.1021/acs.biomac.1c01353  doi:10.3204/PUBDB-2022-01162

Abstract: Human 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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Contributing Institute(s):

1. FPF Functional Protein Fibrils (CSSB-F)
2. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2022

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Database coverage:
; ; BIOSIS Previews ; Biological Abstracts ; Chemical Reactions ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 5 ; Index Chemicus ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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