PROADS

Molecular Recognition: Understanding Proteins Adsorption to Inorganic Surfaces

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 Obiettivo del progetto (Objective)

'Understanding how proteins adsorb to inorganic surfaces is important in many biotechnological applications, including the design of medical implants, fabrication of antibacterial surfaces and biomeneralization. Many studies have been carried out in order to examine how proteins interact with inorganic entities or surfaces; still, it is not clear how proteins “sense” the inorganic surface. The aim of the proposed research is get insights into the fundamental rules that govern protein adsorption. The approach will combine the use of two powerful tools: atomic force spectroscopy and self-assembled monolayers. It will undertake a reductionist methodology and study the adsorption of individual amino acids to chemically well-defined surfaces, functionalized with self-assembled monolayers, using single-molecule spectroscopy. The experimental approach that will be developed, in the course of the project, will be useful as a tool for other researches in the field. Additionally, findings from this research will allow the design of antibacterial surfaces, new biomaterials and peptides that interact with inorganic surfaces or particles in a controlled manner to form composite materials.'

Introduzione (Teaser)

The interaction among different molecules and substrates in nature could be exploited for biomedical applications. Understanding the determinants of these interactions is therefore essential.

Descrizione progetto (Article)

Many biotechnological applications utilise composite materials where proteins interact with inorganic materials. A prime example is the combination of collagen and hydroxyapatite in biomimetic scaffolds that serve as a mechanical and supportive matrix for the formation of bone. Peptides are also incorporated in nano-structured materials with novel properties and functions for surface biocompatibility and drug delivery.

As a result, understanding how proteins interact with inorganic materials should help design effective biomedical materials for a variety of applications. In this context, the EU-funded 'Molecular recognition: Understanding proteins adsorption to inorganic surfaces' (PROADS) project set out to investigate the binding of amino acids onto inorganic substrates.

For this purpose, the consortium established a single molecule force spectroscopy using atomic force microscopy to examine how amino acids with different properties interact with inorganic materials in solution. This method is unique in providing information about peptide-inorganic surface interaction at the molecular level with great detail.

Researchers determined the strength of interactions between the individual amino acid residues and the inorganic substrate, and also observed how this is influenced by the ionic strength of the solution. They found that hydrophobic and electrostatic interactions are the strongest bonds of peptides attaching onto a silicon substrate and mica.

These data were supported by computer simulations that also showed that the binding of the peptide to the substrate is controlled by the relative conformational freedom of the peptide and the substrate in solution. Restricting the movement of the substrate seems to improve the binding efficacy of the peptide.

Taken together, PROADS observations have important ramifications for the design of new composite materials. The generated technology could be used further to study the interaction of other molecules and advance biomedical applications.