LL-37 is the only known human cathelicidin, a class of antimicrobial peptides that regulate the innate immune system. LL-37 assists in wound healing and induction of apoptosis, but it has also been implicated in a broad range of medical disorders including cancer, psoriasis, rheumatoid arthritis, and alzheimer's. LL-37 is known to bind to DNA, protect it from degradation by DNases, and carry it to cellular locations where the DNA may provoke an immune response.  The details of LL-37 binding behavior are not well understood, and we have used fluorescence polarization assays to evaluate LL-37 self-association and binding to dsDNA. In the absence of DNA, we observe an increase in fluorescence polarization with increasing concentration of FAM-labelled LL-37 in the 1-20 µM concentration range.  We interpret this as indicative of the formation of self-complexes. The addition of 24-mer dsDNA oligos further increases fluorescence polarization, and we have performed binding curve analysis of the interaction of LL-37 with a CpG DNA sequence.  In addition, we have performed parallel fluorescence microscopy studies to examine the uptake of LL-37/dsDNA complexes with varied DNA sequences into THP-1 monocytic cells.<br/>

Self-association, dsDNA binding, and uptake of the cathelicidin LL-37 by monocytic cells

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.