Characterizing polyproline II conformational change of collagen superhelix unit on adsorption on gold surface.

Nanoscale Adv

Shanghai Engineering Research Center of Molecular Therapeutics and New Drug Development, Shanghai Frontiers Science Center of Molecule Intelligent Syntheses, School of Chemistry and Molecular Engineering, East China Normal University Shanghai 200062 China

Published: September 2023

AI Article Synopsis

  • The study focuses on how collagen interacts with gold nanoparticles, commonly used in medical applications, emphasizing the need to understand this interaction for better clinical use.
  • The research uses molecular dynamics simulations to analyze the adsorption process of a specific collagen tripeptide on gold surfaces, revealing that charged terminal ends favor adhesion and that multiple tripeptide units can form arch-like structures.
  • The presence of the gold surface alters hydrogen bonding behavior and disrupts the natural collagen conformation, suggesting that optimizing interactions with terminal groups could enhance the development of protein-gold materials for medical purposes.

Article Abstract

The dynamic process of protein binding onto a metal surface is a frequent occurrence as gold nanoparticles are increasingly being used in biomedical applications, including wound treatment and drug transport. Collagen, as a major component of the extracellular matrix, has potentially advantageous biomedical applications, due to its excellent biocompatibility and elasticity properties. Therefore, a mechanistic comprehension of how and which species in collagen interact with gold nanoparticles is a prerequisite for collagen-gold complexes in clinical application. However, the dynamic behavior of collagen with the polyproline II (PPII) conformation on gold sheets at the molecular level is too complex to capture under current experimental conditions. Here, using molecular dynamics simulations, we investigate the adsorption process and conformational behavior of the tripeptide Gly-Pro-Hyp with the repetitive unit of the collagen superhelix on the gold surface as a function of number of repeating units from 1 to 10. The different numbers of repeating units all prefer to approach the gold surface and adsorb charged residues at the C-terminal or N-terminal ends, tending to form arch structures on the gold surface. Compared with the various tripeptide units in solution still retaining the native PPII conformation, the presence of the gold surface affects the formation of hydrogen bonds between the protein and water molecules, thus disrupting the PPII conformation of collagen. Specifically, the interaction between the gold surface and HYP limits the rotation of the dihedral angle of collagen, resulting in a tendency for the PPII conformation of the gold surface to transform to the β-sheet conformation. The results provide an indication of how to improve the interaction between the terminal groups and the gold surface for the design of a bioavailable protein-gold material for medicinal purposes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10521299PMC
http://dx.doi.org/10.1039/d3na00185gDOI Listing

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