TY  - JOUR
AU  - Engelberg, Yizhaq
AU  - Landau, Meytal
TI  - The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure
JO  - Nature Communications
VL  - 11
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Nature Publishing Group UK
M1  - PUBDB-2020-03189
SP  - 3894
PY  - 2020
AB  - Here, we demonstrate the self-assembly of the antimicrobial human LL-37 active core (residues 17–29) into a protein fibril of densely packed helices. The surface of the fibril encompasses alternating hydrophobic and positively charged zigzagged belts, which likely underlie interactions with and subsequent disruption of negatively charged lipid bilayers, such as bacterial membranes. LL-37<sub>17–29</sub> correspondingly forms wide, ribbon-like, thermostable fibrils in solution, which co-localize with bacterial cells. Structure-guided mutagenesis analyses supports the role of self-assembly in antibacterial activity. LL-37<sub>17–29</sub> resembles, in sequence and in the ability to form amphipathic helical fibrils, the bacterial cytotoxic PSMα3 peptide that assembles into cross-α amyloid fibrils. This argues helical, self-assembling, basic building blocks across kingdoms of life and points to potential structural mimicry mechanisms. The findings expose a protein fibril which performs a biological activity, and offer a scaffold for functional and durable biomaterials for a wide range of medical and technological applications.
LB  - PUB:(DE-HGF)16
C6  - pmid:32753597
UR  - <Go to ISI:>//WOS:000561123900003
DO  - DOI:10.1038/s41467-020-17736-x
UR  - https://bib-pubdb1.desy.de/record/442743
ER  -