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Calabretta PJ, Chancellor MC, Torres C, et al. Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy. J Funct Biomater. 2012;3(3):514-27doi: 10.3390/jfb3030514.
Calabretta, P. J., Chancellor, M. C., Torres, C., Abel, G. R., Niehaus, C., Birtwhistle, N. J., Khouderchah, N. M., Zemede, G. H., & Eggers, D. K. (2012). Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy. Journal of functional biomaterials, 3(3), 514-27. https://doi.org/10.3390/jfb3030514
Calabretta, Phillip J, et al. "Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy." Journal of functional biomaterials vol. 3,3 (2012): 514-27. doi: https://doi.org/10.3390/jfb3030514
Calabretta PJ, Chancellor MC, Torres C, Abel GR, Niehaus C, Birtwhistle NJ, Khouderchah NM, Zemede GH, Eggers DK. Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy. J Funct Biomater. 2012 Aug 02;3(3):514-27. doi: 10.3390/jfb3030514. PMID: 24955630; PMCID: PMC4031006.
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J Funct Biomater. 2012 Aug 02;3(3):514-27. doi: 10.3390/jfb3030514.

Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy.

Journal of functional biomaterials

Phillip J Calabretta, Mitchell C Chancellor, Carlos Torres, Gary R Abel, Clayton Niehaus, Nathan J Birtwhistle, Nada M Khouderchah, Genet H Zemede, Daryl K Eggers

Affiliations

  1. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  2. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  3. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  4. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  5. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  6. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  7. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  8. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].
  9. Department of Chemistry, San José State University, San José, CA 95192-0101, USA. [email protected].

PMID: 24955630 PMCID: PMC4031006 DOI: 10.3390/jfb3030514

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 secondary structure of each protein following encapsulation are monitored by circular dichroism spectroscopy. In many cases, silica confinement reduces the fraction of properly-folded protein relative to solution, but addition of a secondary solute or modification of the silica surface leads to an increase in structure. Refinement of the glass surface by addition of a monosubstituted alkoxysilane during sol-gel processing is shown to be a valuable tool for testing the effects of surface chemistry on protein structure. Because silica entrapment prevents protein aggregation by isolating individual protein molecules in the pores of the glass material, one may monitor aggregation-prone polypeptides under solvent conditions that are prohibited in solution, as demonstrated with polyglutamine and a disease-related variant of superoxide dismutase.

References

  1. Biochemistry. 1969 Oct;8(10):4108-16 - PubMed
  2. J Pept Res. 1997 Jul;50(1):73-5 - PubMed
  3. Biochemistry. 2004 May 4;43(17):4899-905 - PubMed
  4. J Biol Chem. 1968 Feb 25;243(4):683-9 - PubMed
  5. Curr Opin Struct Biol. 2010 Apr;20(2):196-206 - PubMed
  6. Annu Rev Biochem. 2005;74:563-93 - PubMed
  7. Trends Biochem Sci. 2001 Oct;26(10):597-604 - PubMed
  8. Curr Opin Struct Biol. 1997 Dec;7(6):828-34 - PubMed
  9. J Biol Chem. 2001 Apr 6;276(14):10577-80 - PubMed
  10. J Mol Biol. 2001 Dec 7;314(4):911-22 - PubMed
  11. Biopolymers. 1992 Feb;32(2):185-8 - PubMed
  12. Protein Sci. 2001 Feb;10(2):250-61 - PubMed
  13. J Mol Cell Biol. 2010 Aug;2(4):180-91 - PubMed
  14. Biosens Bioelectron. 2007 May 15;22(11):2387-99 - PubMed
  15. Arch Biochem Biophys. 2009 Dec;492(1-2):40-7 - PubMed
  16. Chembiochem. 2011 May 2;12(7):1043-8 - PubMed
  17. J Mol Biol. 2001 Aug 3;311(1):173-82 - PubMed
  18. Science. 1992 Feb 28;255(5048):1113-5 - PubMed
  19. J Biol Chem. 2002 May 3;277(18):15932-7 - PubMed
  20. Chem Commun (Camb). 2007 Mar 28;(12):1266-8 - PubMed
  21. Biomaterials. 2008 Jun;29(18):2710-8 - PubMed
  22. Protein Sci. 2001 Apr;10(4):887-91 - PubMed
  23. J Am Chem Soc. 2011 Jun 1;133(21):8082-5 - PubMed
  24. Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5355-8 - PubMed

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