Molecular Dynamics Simulations of a Catalytic Multivalent Peptide-Nanoparticle Complex

Molecular modeling of a supramolecular catalytic system is conducted resulting from the assembling between a small peptide and the surface of cationic self-assembled monolayers on gold nanoparticles, through a multiscale iterative approach including atomistic force field development, flexible docking with Brownian Dynamics and mu s-long Molecular Dynamics simulations. Self-assembly is a prerequisite for the catalysis, since the catalytic peptides do not display any activity in the absence of the gold nanocluster. Atomistic simulations reveal details of the association dynamics as regulated by defined conformational changes of the peptide due to peptide length and sequence. Our results show the importance of a rational design of the peptide to enhance the catalytic activity of peptide-nanoparticle conjugates and present a viable computational approach toward the design of enzyme mimics having a complex structure-function relationship, for technological and nanomedical applications.

Automated summary

The research showed that self-assembly is a prerequisite for the catalysis, and the dynamics of peptide binding to gold nanoparticles are influenced by conformational changes and sequences. Rational design of peptide sequences can enhance catalytic activity, which is crucial for the design of enzyme mimics with a complex structure-function relationship.