High amphipathicity of α-helical peptides enhances unmethylated CpG DNA-induced activation of mouse macrophage-like RAW264.7 cells.

The α-helical antimicrobial peptide Kn2-7 enhances the activation of mouse macrophage-like RAW264.7 induced by DNA containing unmethylated cytosine-guanine motifs (CpG DNA). This enhancement is related to increased cellular uptake of DNA by Kn2-7, but the relevant properties of Kn2-7 are unknown.

A tailored tetravalent peptide displays dual functions to inhibit amyloid β production and aggregation.

Inhibition of amyloid-β peptide (Aβ) accumulation in the brain is a promising approach for treatment of Alzheimer's disease (AD). Aβ is produced by β-secretase and γ-secretase in endosomes via sequential proteolysis of amyloid precursor protein (APP). Aβ and APP have a common feature to readily cluster to form multimers.

Enhanced cellular uptake of CpG DNA by α-helical antimicrobial peptide Kn2-7: Effects on macrophage responsiveness to CpG DNA.

DNA containing unmethylated cytosine-guanine motifs (CpG DNA) initiates innate immune responses, including the secretion of cytokines from macrophages. Some antimicrobial peptides modulate the responses to CpG DNA, although the molecular mechanisms of this process remain unclear. This study examined the effects of four α-helical antimicrobial peptides on the immune responses induced by CpG DNA.