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Biomolecules, Volume 10, Issue 1
January 2020 - 163 articles
Cover Story: In this paper, a combination of theoretical and experimental approaches towards a rational design of amyloid-forming peptides comprising natural beta-sheet cores was used. The peptides were designed to contain positively charged and aromatic residues exposed at key positions in order to promote both DNA condensation and cell internalization. These designer peptide fibrils can efficiently enter mammalian cells while carrying packaged luciferase encoding plasmid DNA and act as a protein expression enhancer. They also exhibited strong antimicrobial activity against E. coli bacteria. Such designer amyloid materials could constitute a stepping stone for using amyloids as novel biomaterial scaffolds which combine cell penetration and gene transfer along with antibacterial properties. View this paper.
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Biomolecules - ISSN 2218-273X