Computational Strategies for Protein-Surface and Protein-Nanoparticle Interactions


  • Giorgia Brancolini Center S3, CNR Institute Nanoscience, Via Campi 213/A, 41125 Modena, Italy
  • Laura Zanetti Polzi Center S3, CNR Institute Nanoscience, Via Campi 213/A, 41125 Modena, Italy
  • Stefano Corni Center S3, CNR Institute Nanoscience, Via Campi 213/A, 41125 Modena, Italy



gold; nanoparticles; amyloid; docking, molecular dynamics, redox potential.


Protein-nanoparticle associations have important applications in nanoscience
and nanotechnology but the recognition mechanisms and the determinants
of specificity are still poorly understood at the microscopic level. Crucial
questions remain open, related to the association mechanisms, control of
binding events, and preservation of functionality. Gold is a promising material
in nanoparticles for nanobiotechnology applications because of the ease of
its functionalization and its tunable optical properties. We present a concise
overview of recent computational modeling advances which were pursued in
the quest for a theoretical framework elucidating the association mechanisms
and the ability to design and control the recognition events of a specific
class of systems, namely, interfaces between polypeptides/proteins and a gold
surface in the presence of water. We select two different methodological
advances, the first related to the effect of surfactants covering the surface
of nanoparticles and altering their interactions with proteins and the second
related to the immobilization of proteins on inorganic surfaces and conserving
their functionality. Both cases, demonstrate how the understanding of the
polypeptide-surface coupling mechanisms is essential to the control of the
process and exploitation for biotechnological and nanotechnological purposes.


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How to Cite

Brancolini, G., Polzi, L. Z., & Corni, S. (2023). Computational Strategies for Protein-Surface and Protein-Nanoparticle Interactions. Journal of Self Assembly and Molecular Electronics, 2(1), 1–26.