期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 22, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/ijms22073624
关键词
molecular dynamics; multiscale modeling; nanozymes; functionalized metal nanoparticles; peptide
资金
- ERC [ERC-CoG-681285]
- Oak Ridge National Laboratory by the Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy [CNMS2018-338, CNMS2020-B-00433]
- Office of Science of the U.S. Department of Energy [DE-AC02-05CH11231]
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.
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.
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