DOI: 10.1039/9781788010160-00126
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CHAPTER 6. Immobilization of Proteins on Diatom Biosilica

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Cited by 8 publications
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“…A key goal of diatom based materials synthesis is the development of cell lines that produce biosilica with structures and properties tailored for specific applications. Recently, a genetic engineering based method called live diatom silica incorporation (LiDSI) was established that allows for generating diatom strains, which contain desired fluorescent proteins, receptor proteins, or enzymes in the biosilica [31]. While biosilica functionalization using LiDSI is well developed and even enables regioselective incorporation of proteins [32], the genetic engineering of biosilica structure is still in its infancy.…”
Section: Introductionmentioning
confidence: 99%
“…A key goal of diatom based materials synthesis is the development of cell lines that produce biosilica with structures and properties tailored for specific applications. Recently, a genetic engineering based method called live diatom silica incorporation (LiDSI) was established that allows for generating diatom strains, which contain desired fluorescent proteins, receptor proteins, or enzymes in the biosilica [31]. While biosilica functionalization using LiDSI is well developed and even enables regioselective incorporation of proteins [32], the genetic engineering of biosilica structure is still in its infancy.…”
Section: Introductionmentioning
confidence: 99%
“…Immobilization of proteins onto a solid support material allows improving their functionality by stabilizing their native conformation, which is of great benefit in several applications like catalysis, sensing, and drug delivery [84]. Diatom biosilica, in particular, offers several advantages if used as support material: its porosity, characterized by high values of specific surface area (up to 220 m 2 g −1 ), provides a large capacity for binding proteins and a very effective interaction with several adsorbates [53]; the size of frustule pores is large enough to allow for the incorporation of protein molecules, which have an equivalent hydrodinamic diameter of the order of nanometers [85]; its high chemical and mechanical stability and its hydrophilic properties allow for hydrogen bonds and electrostatic interactions with proteins; its transparency in a wide interval of the visible and infrared spectrum make it possible to analyze the immobilized proteins by optical spectroscopy; finally, its biocompatibility allows for in vivo applications.…”
Section: Fustule Functionalization For Protein Immobilizationmentioning
confidence: 99%
“…When electrostatic attraction is the driving force, the adsorption process is highly influenced by environmental conditions such as pH and ionic strength as the ions in solution can shield the charges on the surface of both the protein and the surface. For example, proteins with a net positive charge, which have a surface rich in arginine residues but poor in aromatic ones and are characterized by a low structural rigidity, are more prone to adsorption to the negatively charged hydroxyl-rich surface of biosilica [ 34 , 35 ]. Although the analysis of a protein’s structural features may be complex, it can offer hints as to the optimal immobilization strategy.…”
Section: Protein Structure Surface and Materials Surfacesmentioning
confidence: 99%