By developing a sophistication of the diffusion map nonlinear manifold learning approach, Rachael and Prof. Ferguson have quantitatively connected the molecular chemistry and experimental conditions to microscopic molecular behavior. In a manuscript published in JCP (http://dx.doi.org/10.1063/1.4914144) Rachael has exposed the molecular mechanism by which decreasing side chain length destabilizes the alpha-helical form of synthetic antimicrobial peptides, bringing new microscopic understanding to this fascinating class of peptides. We are now woking with JJ Cheng’s lab to guide the rational design of cell penetrating peptides with tailored stability capable of triggered drug release upon passing through the microbial membrane. Congratulations to Rachael!
Ferguson Lab > Uncategorized > Rachael Mansbach publishes paper on the structural mechanism of the helix-coil transition in alpha-helical peptides with antimicrobial activity in the Journal of Chemical Physics