In the past year we have made significant progress on our work on mimetic peptides of apoA-I and apoC-II. In regard to apoA-I mimetic peptides, we previously discovered that the formation of an amphipathic helix is critical for their ability to remove excess cellular cholesterol by the ABCA1 transporter. Short synthetic peptides, however, frequently are in a random coil configuration and hence are relatively inefficient in effluxing cholesterol from cells. In a paper we published last year in Scientific Reports, we discovered that replacement of the hydrogen attached to the alpha-chiral position of amino acids with a methyl group for not only Alanine but several other amino acids enhances the helicity of peptides and also confers proteolytic resistance. This modification will likely prove to be useful in the design of many other short synthetic peptides. For our project related to apoC-II mimetic peptides, which lower plasma triglycerides by activating Lipoprotein Lipase, we identified a lead peptide to undergo future drug development. This was done in conjunction with Corvidia Inc, which we have a CRADA. We also filed several patents listed below on the new peptide, which is more potent that the full length protein and likely less immunogenic than our earlier generation of apoC-II mimetic peptides.
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