2012
DOI: 10.3390/jfb3030514
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Silica as a Matrix for Encapsulating Proteins: Surface Effects on Protein Structure Assessed by Circular Dichroism Spectroscopy

Abstract: The encapsulation of biomolecules in solid materials that retain the native properties of the molecule is a desired feature for the development of biosensors and biocatalysts. In the current study, protein entrapment in silica-based materials is explored using the sol-gel technique. This work surveys the effects of silica confinement on the structure of several model polypeptides, including apomyoglobin, copper-zinc superoxide dismutase, polyglutamine, polylysine, and type I antifreeze protein. Changes in the … Show more

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Cited by 5 publications
(4 citation statements)
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“…This study, in line with previous findings, suggests that the final products of Si 3 N 4 surface hydrolysis, namely, nitrogen radicals and deprotonated silanols, are key in SARS-CoV-2 viral inactivation. The silanol moieties induce deimination of positively charged arginine to form uncharged citrulline, as proven by studies of protein citrullination on silica particles in an aqueous environment. , On the other hand, nitrogen radicals induce oxidation of free and peptide-bound methionine to form sulfoxide with a conformational switch toward β-sheet structures, nitration of tyrosine residues with the formation of nitrotyrosine (altering hydrogen bonding interactions with the polar hydroxyl groups key in determining the level of infectivity), and breakage of the imidazole ring in RNA purines to form Fapy structures. Obviously, structural and genomic differences have an impact on the extent of structural damage that a given variant could sustain before losing its infectivity.…”
Section: Discussionmentioning
confidence: 99%
“…This study, in line with previous findings, suggests that the final products of Si 3 N 4 surface hydrolysis, namely, nitrogen radicals and deprotonated silanols, are key in SARS-CoV-2 viral inactivation. The silanol moieties induce deimination of positively charged arginine to form uncharged citrulline, as proven by studies of protein citrullination on silica particles in an aqueous environment. , On the other hand, nitrogen radicals induce oxidation of free and peptide-bound methionine to form sulfoxide with a conformational switch toward β-sheet structures, nitration of tyrosine residues with the formation of nitrotyrosine (altering hydrogen bonding interactions with the polar hydroxyl groups key in determining the level of infectivity), and breakage of the imidazole ring in RNA purines to form Fapy structures. Obviously, structural and genomic differences have an impact on the extent of structural damage that a given variant could sustain before losing its infectivity.…”
Section: Discussionmentioning
confidence: 99%
“…The process is nearly bio-compatible, allows for good control of pH and ionic strength and is applicable to variety of biomolecules. 1,2 Specically, nanostructured porous silica matrices are well-known for their excellent payload capacity for proteins/ peptides, [3][4][5][6][7] nucleic acids (DNA, RNA), 8,9 nucleic acid aptamers 10 and microRNA specimens. 11 Despite the success over the last three decades, the inherently complex nature of conventional sol-gel methods makes them hardly applicable to clinical setting.…”
Section: Introductionmentioning
confidence: 99%
“…Since the 1990s, Dunn and coworkers introduced modifications to the sol-gel procedure to prevent the adverse effects of pH and alcohol on enzyme stability [4]. Despite the optimization of sol-gel protocols, silica gel confinement is reported to promote in some cases protein denaturation For this reason, additional solutes or modified silica surfaces can be introduced to stabilize the protein [5]. Examples of stabilizers are Ca 2+ [36,37], organosilanes [38,39], polyethylene glycol (PEG) [40], graft copolymers [41][42][43] and charged polymers [44,45].…”
Section: Preserving Protein Functionmentioning
confidence: 99%
“…Encapsulation of proteins in silica gels prepared through the sol-gel method began in the 1990s [2][3][4]. Although there are reports indicating reversible, protocol-dependent changes in the secondary structure of some proteins and model peptides [5][6][7], *Address correspondence to this author at the Department of Neurosciences, University of Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy; Tel: +39 0521 905502; Fax: +39 0521 905151; E-mail: stefano.bettati@unipr.it proteins encapsulated in silica gels normally retain their native conformation and spectroscopic properties. Function can be retained completely or partially, or even increased when the gel matrix stabilizes active conformations and/or provides a favorable environment for enzyme catalysis.…”
Section: Introductionmentioning
confidence: 99%