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Received April 7, 2012
Accepted May 4, 2012
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Techniques for monitoring protein misfolding and aggregation in vitro and in living cells
1Department of Chemical Engineering, University of Virginia, Charlottesville, Virginia 22904, USA 2Institutes on Aging, University of Virginia, Charlottesville, Virginia 22904, USA
ik4t@virginia.edu
Korean Journal of Chemical Engineering, June 2012, 29(6), 693-702(10), 10.1007/s11814-012-0060-x
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Abstract
Protein misfolding and aggregation have been considered important in understanding many neurodegenerative diseases and recombinant biopharmaceutical production. Various traditional and modern techniques have been utilized to monitor protein aggregation in vitro and in living cells. Fibril formation, morphology and secondary structure content of amyloidogenic proteins in vitro have been monitored by molecular probes, TEM/AFM, and CD/FTIR analyses, respectively. Protein aggregation in living cells has been qualitatively or quantitatively monitored by numerous_x000D_
molecular folding reporters based on either fluorescent protein or enzyme. Aggregation of a target protein is directly correlated to the changes in fluorescence or enzyme activity of the folding reporter fused to the target protein, which allows non-invasive monitoring aggregation of the target protein in living cells. Advances in the techniques used to monitor protein aggregation in vitro and in living cells have greatly facilitated the understanding of the molecular mechanism of amyloidogenic protein aggregation associated with neurodegenerative diseases, optimizing culture conditions to reduce aggregation of biopharmaceuticals expressed in living cells, and screening of small molecule libraries in the search for protein aggregation inhibitors.
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Necula M, Kayed R, Milton S, Glabe CG, J. Biol. Chem., 282, 10311 (2007)
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Lee D, Lee EK, Lee JH, Chang CS, Paik SR, Eur. J. Biochem., 268, 295 (2001)
Ha C, Park CB, Biotechnol. Bioeng., 90(7), 848 (2005)
Ku SH, Park CB, Langmuir, 24(24), 13822 (2008)
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Dasilva KA, Shaw JE, McLaurin J, Exp. Neurol., 223, 311 (2010)
Gras SL, Waddington LJ, Goldie KN, Notes., 752, 197 (2011)
Toyama BH, Weissman JS, Annu. Rev. Biochem., 80, 557 (2011)
Langkilde AE, Vestergaard B, Febs Lett., 583, 2600 (2009)
Chimon S, Shaibat MA, Jones CR, Calero DC, Aizezi B, Ishii Y, Nat. Struct. Mol. Biol., 14, 1157 (2007)
Stine WB, Dahlgren KN, Krafft GA, LaDu MJ, The Journal of Biological Chemistry., 278, 11612 (2003)
Perczel A, Park K, Fasman GD, Proteins: Structure, Function, and Bioinformatics., 13, 57 (1992)
Whitmore L, Wallace BA, Biopolymers., 89, 392 (2008)
Bartolini M, Bertucci C, Bolognesi ML, Cavalli A, Melchiorre C, Andrisano V, Chembiochem: A European Journal of Chemical Biology., 8, 2152 (2007)
Greenfield NJ, Trends in Analytical Chemistry., 18, 236 (1999)
Pelton JT, McLean LR, Anal. Biochem., 277, 167 (2000)
Surewicz WK, Mantsch JHH, Chapman D, Biochemistry., 32 (1993)
Correa DHA, Ramos CHI, J. Biochem., 3, 164 (2009)
Soto C, Castan EM, J. Biochem., 314, 701 (1996)
Vieira EP, Hermel H, Mohwald H, Biochim. Biophys. Acta., 1645, 6 (2003)
Tomaselli S, Esposito V, Vangone P, van Nuland, NAJ, Bonvin AMJJ, Guerrini R, Tancredi T, Temussi PA, Picone D, Chembiochem: A European Journal of Chemical Biology., 7, 257 (2006)
Greenfield NJ, Nature Protocols., 1, 2876 (2006)
Kim W, Hecht MH, J. Biol. Chem., 280, 35069 (2005)
Kim W, Hecht MH, J. Mol. Biol., 377, 565 (2008)
Arslan PE, Chakrabartty A, Biochem. Cell Biol., 87, 631 (2009)
Arslan PE, Mulligan VK, Ho S, Chakrabartty A, J. Mol. Biol., 396, 1284 (2010)
Heddle C, Mazaleyrat SL, Protein. Eng. Des. Sel., 20, 327 (2007)
Gregoire S, Kwon I, ACS Meeting., 234-BIOT, 241 (2011)
Kim W, Kim Y, Min J, Kim DJ, Chang YT, Hecht MH, ACS Chem. Biol., 1, 461 (2006)
Geng J, Li M, Ren J, Wang E, Qu X, Angew. Chem. Int. Ed. Eng., 50, 4184 (2011)
Philipps B, Hennecke J, Glockshuber R, J. Mol. Biol., 327, 239 (2003)
Cabantous S, Terwilliger TC, Waldo GS, Nat. Biotechnol., 23, 102 (2005)
Cabantous S, Pedelacq JD, Mark BL, Naranjo C, Terwilliger TC, Waldo GS, J. Struct. Funct. Genomics., 6, 113 (2005)
Cabantous S, Waldo GS, Nat. Methods., 3, 845 (2006)
Chun WJ, Waldo GS, Johnson GVW, J. Neurochem., 103, 2529 (2007)
Listwan P, Terwilliger TC, Waldo GS, J. Struct. Funct. Genomics., 10, 47 (2009)
Lockard MA, Listwan P, Pedelacq JD, Cabantous S, Nguyen HB, Terwilliger TC, Waldo GS, Protein Engineering Design & Selection., 24, 565 (2011)
Maxwell KL, Mittermaier AK, Forman-Kay JD, Davidson AR, Protein Sci., 8, 1908 (1999)
Dyson MR, Perera RL, Shadbolt SP, Biderman L, Bromek K, Murzina NV, McCafferty J, Nucleic Acids Res., e51.Epub 2008 Apr 17., 36 (2008)
Dyson MR, Biochem. Soc. Trans., 38, 908 (2010)
Morell M, de Groot NS, Vendrell J, Aviles FX, Ventura S, Mol. Biosyst., 7, 1121 (2011)
Wigley WC, Stidham RD, Smith NM, Hunt JF, Thomas PJ, Nat. Biotechnol., 19, 131 (2001)
Foit L, Morgan GJ, Kern MJ, Steimer LR, von Hacht AA, Titchmarsh J, Warriner SL, Radford SE, Bardwell JC, Mol. Cell., 36, 861 (2009)
Mansell TJ, Linderman SW, Fisher AC, DeLisa MP, Protein Science., 19, 1079 (2010)
Mansell TJ, Fisher AC, DeLisa MP, Curr. Protein Peptide Sci., 9, 138 (2008)
Yumerefendi H, Tarendeau F, Mas PJ, Hart DJ, J. Struct. Biol., 172(1), 66 (2010)
An Y, Yumerefendi H, Mas PJ, Chesneau A, Hart DJ, J.Struct. Biol., 175, 189 (2011)
Nolting B, Methods in modern biophysics: Ch. 5 - protein infrared spectroscopy, Springer Berlin Heidelberg, 91 (2010)
Wiseman RL, Kelly JW, Mol. Cell., 36, 730 (2009)
