Ethyl 3-Ethoxypropionate Synthesis Essay

The interaction between proteins and inorganic minerals leads to the construction of composite materials with distinctive properties. This includes materials with high mechanical strength or unique optical properties.1,2 For example, the combination of the protein collagen with the mineral hydroxyapatite generates either soft or hard bones for different functionalities.3 Short peptides can also bind inorganic materials with high specificity.4,5,6 The specificity of these peptides has been used for designing new magnetic and electronic materials,7,8,9 fabricating nanostructured materials, growing crystals,10 and synthesizing nanoparticles.11Understanding the mechanism underlying interactions between peptides or proteins and inorganic materials will therefore allow us to design new composite materials with improved adsorptive properties. In addition, since the interphase of implants with an immune response is mediated by proteins, better understanding the interactions of proteins with inorganic materials will improve our ability to design implants. Another important area that involves proteins interacting with inorganic surfaces is the fabrication of antifouling materials.12,13,14,15 Biofouling is an undesirable process in which organisms attach to a surface. It has many detrimental implications on our lives. For example, biofouling of bacteria on medical devices leads to hospital-acquired infections. Biofouling of marine organisms on boats and large ships increases the consumption of fuel.12,16,17,18

Single-molecule force spectroscopy (SMFS), using an AFM, can directly measure the interactions between an amino acid or a peptide with a substrate.19,20,21,22,23,24,25,26 Other methods such as phage display,27,28quartz crystal microbalance (QCM)29or surface plasmon resonance (SPR)29,30,31,32,33 measure the interactions of peptides and proteins to inorganic surfaces in bulk.34,35,36This means that the results obtained by these methods relate to ensembles of molecules or aggregates. In SMFS, one or very few molecules are fixed to the AFM tip and their interactions with the desired substrate is measured. This approach can be expanded to study protein folding by pulling the protein from the surface. In addition, it can be used to measure interactions between cells and proteins and the binding of antibodies to their ligands.37,38,39,40 This paper describes in detail how to attach either peptides or amino acids to the AFM tip using silanol chemistry. In addition, the paper explains how to perform force measurements and how to analyze the results.

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