a biotech company designing antimicrobial peptides
we are facing a worldwide re-emergence of infectious diseases threatening the world with return to the pre-antibiotic era.
There are now “Superbugs” that are resistant to most or all available antibiotics, including antibiotics of last resort. If proactive solutions are not quickly found to slow the rate of drug resistance, it has been estimated that by 2050, ten million lives a year will be at risk. Currently, 700,000 people die every year from drug resistant strains of common bacterial infections, HIV, TB and malaria. Even in developed countries such as the United States, each year about 2 million people become infected with antibiotic-resistant bacteria resulting in at least 23,000 deaths annually. A conservative estimate for the global marketplace for healthcare-associated infections (HAIs) caused by Gram-negative bacteria across the seven major pharmaceutical markets is projected to exceed US$3.6 billion in sales by 2026.
Our de novo rational design platform has produced a large portfolio of D-conformation, α-helical antimicrobial peptides that are structurally manipulated to alter their hydrophobicity and amphipathicity properties. Positively charged substitutions and structural alterations on both the polar and non-polar faces of our peptides produce a unique “carpet model” mechanism of action. Our membrane-discriminate peptides are:
We deploy positive charge substitution on the non-polar face (“specificity determinants”) to facilitate cytoplasmic membrane selectivity for Gram-negative prokaryotic organisms.
Our discovery of specificity determinants coupled with substitution of unusual charged amino acids (Dab and Dap) on the polar face eliminates toxicity towards eukaryotic cells as determined by the most stringent conditions of hemolysis of human red blood cells. Such results are unprecedented in AMP research.
Unlike L-conformation forms, our D-conformation peptides are resistant to proteolytic enzymes, providing extended circulating half-lives.