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    University - Student Department: Computer Science Position: Graduate

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All Publications

  • A biofilm-targeting lipo-peptoid to treat Pseudomonas aeruginosa and Staphylococcus aureus co-infections Biofilm Wardell, S. J., Yung, D. B., Nielsen, J. E., Lamichhane, R., Sørensen, K., Molchanova, N., Herlan, C., Lin, J. S., Bräse, S., Wise, L. M., Barron, A. E., Pletzer, D. 2025; 9: 13

    View details for DOI 10.1016/j.bioflm.2025.100272

  • Upregulating Human Cathelicidin Antimicrobial Peptide LL-37 Expression May Prevent Severe COVID-19 Inflammatory Responses and Reduce Microthrombosis Frontiers in Immunology Aloul, K. M., Nielsen, J. E., Defensor, E. B., Lin, J. S., Fortkort, J. A., Shamloo, M., Cirillo, J. D., Gombart, A. F., Barron, A. E. 2022; 13: 1-16

    View details for DOI 10.3389/fimmu.2022.880961

  • Potent Antiviral Activity against HSV-1 and SARS-CoV-2 by Antimicrobial Peptoids Pharmaceuticals Diamond, G., Molchanova, N., Herlan, C., Fortkort, J. A., Lin, J. S., Figgins, E., Bopp, N., Ryan, L. K., Chung, D., Adcock, R. S., Sherman, M., Barron, A. E. 2021; 14 (4): 304

    View details for DOI 10.3390/ph14040304

  • Evidence that the Human Innate Immune Peptide LL-37 may be a Binding Partner of Amyloid-β and Inhibitor of Fibril Assembly Journal of Alzheimer's Disease De Lorenzi, E., Chiari, M., Colombo, R., Cretich, M., Sola, L., Vanna, R., Gagni, P., Bisceglia, F., Morasso, C., Lin, J. S., Lee, M., McGeer, P. L., Barron, A. E. 2017; 59 (4): 1213-1226

    Abstract

    Identifying physiologically relevant binding partners of amyloid-β (Aβ) that modulate in vivo fibril formation may yield new insights into Alzheimer's disease (AD) etiology. Human cathelicidin peptide, LL-37, is an innate immune effector and modulator, ubiquitous in human tissues and expressed in myriad cell types.We present in vitro experimental evidence and discuss findings supporting a novel hypothesis that LL-37 binds to Aβ42 and can modulate Aβ fibril formation.Specific interactions between LL-37 and Aβ (with Aβ in different aggregation states, assessed by capillary electrophoresis) were demonstrated by surface plasmon resonance imaging (SPRi). Morphological and structural changes were investigated by transmission electron microscopy (TEM) and circular dichroism (CD) spectroscopy. Neuroinflammatory and cytotoxic effects of LL-37 alone, Aβ42 alone, and LL-37/Aβ complexes were evaluated in human microglia and neuroblastoma cell lines (SH-SY5Y).SPRi shows binding specificity between LL-37 and Aβ, while TEM shows that LL-37 inhibits Aβ42 fibril formation, particularly Aβ's ability to form long, straight fibrils characteristic of AD. CD reveals that LL-37 prevents Aβ42 from adopting its typical β-type secondary structure. Microglia-mediated toxicities of LL-37 and Aβ42 to neurons are greatly attenuated when the two peptides are co-incubated prior to addition. We discuss the complementary biophysical characteristics and AD-related biological activities of these two peptides.Based on this body of evidence, we propose that LL-37 and Aβ42 may be natural binding partners, which implies that balanced (or unbalanced) spatiotemporal expression of the two peptides could impact AD initiation and progression.

    View details for DOI 10.3233/JAD-170223

    View details for PubMedCentralID PMC5611894