anti-infective activity of apolipoprotein domain derived peptides in vitro identification of novel antimicrobial peptides related to apolipoprotein b with anti-hiv activity抗感染药载脂蛋白的活动领域衍生肽体外鉴定新型抗菌肽与载脂蛋白b与抗艾滋病活动有关.pdfVIP

Kelly et al. BMC Immunology 2010, 11:13 /1471-2172/11/13 RESEARCH ARTICLE Open Access Anti-infective activity of apolipoprotein domain derived peptides in vitro: identification of novel antimicrobial peptides related to apolipoprotein B with anti-HIV activity 1 2 2 1* Bridie A Kelly , Ian Harrison , Áine McKnight , Curtis B Dobson Abstract Background: Previous reports have shown that peptides derived from the apolipoprotein E receptor binding region and the amphipathic a-helical domains of apolipoprotein AI have broad anti-infective activity and antiviral activity respectively. Lipoproteins and viruses share a similar cell biological niche, being of overlapping size and displaying similar interactions with mammalian cells and receptors, which may have led to other antiviral sequences arising within apolipoproteins, in addition to those previously reported. We therefore designed a series of peptides based around either apolipoprotein receptor binding regions, or amphipathic a-helical domains, and tested these for antiviral and antibacterial activity. Results: Of the nineteen new peptides tested, seven showed some anti-infective activity, with two of these being derived from two apolipoproteins not previously used to derive anti-infective sequences. Apolipoprotein J (151-170) - based on a predicted amphipathic alpha-helical domain from apolipoprotein J - had measurable anti-HSV1 activity, as did apolipoprotein B (3359-3367) dp (apoBdp), the latter being derived from the LDL receptor binding domain B of apolipoprotein B. The more active peptide - apoBdp - showed similarity to the previously reported apoE derived anti-infective peptide, and further modification of the