In this proposal, a scheme is outlined to develop multi-scale modeling efforts of peptide-drug amphiphiles in direct collaboration with an experimental group. Peptide drug-amphiphiles self- assemble into cylindrical fibers with unique characteristics - high drug loading and morphological tunability. Particularly interesting is the ability to tune the peptide sequence to optimize the mechanical properties (persistence length) of the fibers. Control of the persistence length of the fibers should allow for the optimization of the circulation time in the blood-stream. Furthermore, the ability to tune the persistence length and shape (such as helicity) of the fibers will provide for a method to optimize the interaction with and across the cellular membrane. Insight gained should inform the design of novel anticancer drug delivery systems.
State-of-the-art simulation and modeling techniques will be used to molecularly design and predict the structure and stability of peptide-drug amphiphiles, including their interaction with model cellular membranes. Insight gained should inform the design of novel delivery systems.
| Kang, Myungshim; Chakraborty, Kaushik; Loverde, Sharon M (2018) Molecular Dynamics Simulations of Supramolecular Anticancer Nanotubes. J Chem Inf Model 58:1164-1168 |
| Kang, Myungshim; Cui, Honggang; Loverde, Sharon M (2017) Coarse-grained molecular dynamics studies of the structure and stability of peptide-based drug amphiphile filaments. Soft Matter 13:7721-7730 |
| Manandhar, Anjela; Kang, Myungshim; Chakraborty, Kaushik et al. (2017) Molecular simulations of peptide amphiphiles. Org Biomol Chem 15:7993-8005 |
