(703f) Ibuprofen Loading and Release in Micelles Formed By Amphiphilic Peptide (AF)6H5K15: A Coarse-Grained Molecular Dynamics Simulation

Thota, N. - Presenter, National University of Singapore
Jiang, J., National University of Singapore
Hu, Z., Bioinformatics Institute, A*STAR

Amphiphilic peptides have been recognized as good candidates for drug delivery due to their self-assembly nature. We report a molecular dynamics simulation study for drug (ibuprofen) loading and release in micelles formed by peptide (AF)6H5K15 (FA32). The peptide, drug, water and counterions are represented by the MARTINI coarse-grained model. With 5 µs simulation duration, ibuprofen is loaded into the micelle core and covered by peptide residues. Upon protonating Histidine residues and along with applying an external force on solvent to mimic stirring effect, ibuprofen is observed to be released. This suggests that the drug can be released from the micellar core when it reaches the vicinity of tumor cells with an acidic pH. The microscopic insight from molecular simulation is helpful to better understand the mechanisms of drug loading and release, and could facilitate the development of new amphiphilic peptides for high-efficacy drug delivery.