New Paper: Controlling Membrane Active Peptide Activity

Hello Everyone,

I’m happy to say that I was able to publish what was the bulk of my PhD thesis work in the Journal of the American Chemical Society and that it is finally available.  This work formed the initial basis of my ideas around Molecular Yoga, the ability to control the ways in which molecules can change conformation and activate certain functions.  In short, we created a combinatorial library based on the membrane active, toxic peptide Super-Melittin (derived from Melittin from honeybee venom).  This peptide has excellent antimicrobial and potent anti-cancer capabilities but it is very harmful to our own body’s cells as well.  I believe that by changing just a few of the amino acids we could create a peptide that would be inactive at neutral pH but could fold into an alpha-helix and activate at a low pH.  Low pH environments are often found in tumors and with fungi and bacteria, making it an good activating key for these peptides.  We’re currently working to develop a patent for these exact purposes and some of my colleagues, Sarah and Elmer are still working very hard to improve these peptides further.  Please give it a read and let me know what you think!

I have another announcement too.  I’ll be reporting next month as part of the 61st Biophysical Society Meeting blog in New Orleans.  I hope to use this as a way to bring science to the public and to help them to interact with the scientific community.  Look for updates along these lines in the next few weeks!  Thanks for reading!





pH-Triggered, Macromolecule-Sized Poration of Lipid Bilayers by Synthetically Evolved Peptides. Wiedman G, Kim SY, Zapata-Mercado E, Wimley WC, Hristova K. (2016)  JACS