![]() ![]() Antimicrobial peptides (AMPs) are canonical components of the innate immune system of many organisms 9. One such application is addressing the urgent need to fight microbial aggressive, resistance, infections using materials which allow oral bioavailability, stability in harsh conditions, and long shelf-life. The assembly of basic biological molecules into filamentous structures provides ample opportunities to design bioinspired materials for medical and technological applications 1, 2, 3, 4, 5, 6, 7, 8. ![]() 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. This argues helical, self-assembling, basic building blocks across kingdoms of life and points to potential structural mimicry mechanisms. LL-37 17–29 resembles, in sequence and in the ability to form amphipathic helical fibrils, the bacterial cytotoxic PSMα3 peptide that assembles into cross-α amyloid fibrils. Structure-guided mutagenesis analyses supports the role of self-assembly in antibacterial activity. LL-37 17–29 correspondingly forms wide, ribbon-like, thermostable fibrils in solution, which co-localize with bacterial cells. 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. ![]() 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. ![]()
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |