TY  - JOUR
AU  - Engelberg, Yizhaq
AU  - Ragonis-Bachar, Peleg
AU  - Landau, Meytal
TI  - Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides
JO  - Biomacromolecules
VL  - 23
IS  - 3
SN  - 1525-7797
CY  - Columbus, Ohio
PB  - American Chemical Soc.
M1  - PUBDB-2022-01162
SP  - 926 – 936
PY  - 2022
AB  - Human LL-37<sub>17–29</sub> is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-37<sub>17–29</sub> 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<sub>17–29</sub> 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.
LB  - PUB:(DE-HGF)16
C6  - 35061360
UR  - <Go to ISI:>//WOS:000813069600001
DO  - DOI:10.1021/acs.biomac.1c01353
UR  - https://bib-pubdb1.desy.de/record/475051
ER  -