Abstract
The combination of infrared spectroscopy and isotope labeling is a powerful toolset for providing residue-specific information about the structure and aggregation kinetics of amyloid peptides. In this chapter, we review a simple mathematical formalism to guide the interpretation of 1D- and 2DIR spectra of amyloid fibers. This formalism enables the design of isotope labeling schemes to extract precise structural features from IR spectra. We present 2DIR experiments on hIAPP and Aβ in which some of these strategies have been employed.
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References
J.J. Meier, R. Kayed, C.-Y. Lin, T. Gurlo, L. Haataja, S. Jayasinghe, R. Langen, C.G. Glabe, P.C. Butler, Am. J. Physiol. Endocrinol. Metab. 291, E1317 (2006)
A.E. Butler, J. Janson, W.C. Soeller, P.C. Butler, Diabetes 52, 2304 (2003)
S.A. Petty, S.M. Decatur, J. Am. Chem. Soc. 127, 13488 (2005)
R.A. Gangani, D. Silva, W. Barber-Armstrong, S.M. Decatur, J. Am. Chem. Soc. 125, 13674 (2003)
S.A. Petty, S.M. Decatur, Proc. Natl. Acad. Sci. U.S.A. 102, 14272 (2005)
S.M. Decatur, Acc. Chem. Res. 39, 169 (2006)
Y.S. Kim, L. Liu, P.H. Axelsen, R.M. Hochstrasser, Proc. Natl. Acad. Sci. U.S.A. 105, 7720 (2008)
Y.S. Kim, L. Liu, P.H. Axelsen, R.M. Hochstrasser, Proc. Natl. Acad. Sci. U.S.A. 106, 17751 (2009)
D.B. Strasfeld, Y.L. Ling, R. Gupta, D.P. Raleigh, M.T. Zanni, J. Phys. Chem. B 113, 15679 (2009)
S.-H. Shim, R. Gupta, Y.L. Ling, D.B. Strasfeld, D.P. Raleigh, M.T. Zanni, Proc. Natl. Acad. Sci. U.S.A. 106, 6614 (2009)
C.T. Middleton, A.M. Woys, S. Mukherjee, M.T. Zanni, Methods 52, 12 (2010)
S. Mukherjee, P. Chowdhury, F. Gai, J. Phys. Chem. B 111, 4596 (2007)
S. Mukherjee, P. Chowdhury, F. Gai, J. Phys. Chem. B 113, 531 (2009)
D.H.J. Lopes, A. Meister, A. Gohlke, A. Hauser, A. Blume, R. Winter, Biophys. J. 93, 3132 (2007)
S. Jha, D. Sellin, R. Seidel, R. Winter, J. Mol. Biol. 389, 907 (2009)
D.L. Sellin, L.-M. Yan, A. Kapurniotu, R. Winter, Biophys. Chem. 150, 73 (2010)
S. Luca, W.-M. Yau, R. Leapman, R. Tycko, Biochemistry 46, 13505 (2007)
A.S. Reddy, L. Wang, S. Singh, Y.L. Ling, L. Buchanan, M.T. Zanni, J.L. Skinner, J.J. de Pablo, Biophys. J. 99, 2208 (2010)
A.S. Reddy, L. Wang, Y.-S. Lin, Y. Ling, M. Chopra, M.T. Zanni, J.L. Skinner, J.J. de Pablo, Biophys. J. 98, 443 (2010)
W. Zhuang, D. Abramavicius, T. Hayashi, S. Mukamel, J. Phys. Chem. B 110, 3362 (2006)
S. Bagchi, C. Falvo, S. Mukamel, R.M. Hochstrasser, J. Phys. Chem. B 113, 11260 (2009)
N. Sengupta, H. Maekawa, W. Zhuang, C. Toniolo, S. Mukamel, D.J. Tobias, N.-H. Ge, J. Phys. Chem. B 113, 12037 (2009)
J.-H. Choi, S. Ham, M. Cho, J. Phys. Chem. B 107, 9132 (2003)
C. Lee, M. Cho, J. Phys. Chem. B 108, 20397 (2004)
S. Hahn, S. Kim, C. Lee, M. Cho, J. Chem. Phys. 123, 084905 (2005)
P. Hamm, M.T. Zanni, Concepts and Methods of 2D Infrared Spectroscopy (Cambridge University Press, Cambridge, 2011)
A.M. Woys, Y.S. Lin, A.S. Reddy, W. Xiong, J.J. de Pablo, J.L. Skinner, M.T. Zanni, J. Am. Chem. Soc. 132, 2832 (2010)
Y.L. Ling, D.B. Strasfeld, S.-H. Shim, D.P. Raleigh, M.T. Zanni, J. Phys. Chem. B 113, 2498 (2009)
P. Marek, A.M. Woys, K. Sutton, M.T. Zanni, D.P. Raleigh, Org. Lett. 12, 4848 (2010)
S.-H. Shim, D.B. Strasfeld, Y.L. Ling, M.T. Zanni, Proc. Natl. Acad. Sci. U.S.A. 104, 14197 (2007)
S.-H. Shim, M.T. Zanni, Phys. Chem. Chem. Phys. 11, 748 (2009)
E.M. Grumstrup, S.-H. Shim, M.A. Montgomery, N.H. Damrauer, M.T. Zanni, Opt. Express 15, 16681 (2007)
H. Naiki, K. Higuchi, M. Hosokawa, T. Takeda, Anal. Biochem. 177, 244 (1989)
H. Naiki, K. Higuchi, K. Nakakuki, T. Takeda, Lab Invest. 65, 104 (1991)
Y.C. Kudva, C. Mueske, P.C. Butler, N.L. Eberhardt, Biochem. J. 331, 809 (1998)
S.B. Padrick, A.D. Miranker, Biochemistry 41, 4694 (2002)
Acknowledgements
The authors would like to acknowledge Sang-hee Shim, David Strasfeld, and Yun Ling who contributed much of the data on hIAPP presented in this chapter and Yung Sam Kim and Robin Hochstrasser for providing the data on Aβ. We would also like to acknowledge our collaborators Juan de Pablo and Jim Skinner as well as funding from the NSF CHE-0832584 and NIH DK079895.
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Buchanan, L.E., Dunkelberger, E.B., Zanni, M.T. (2012). Examining Amyloid Structure and Kinetics with 1D and 2D Infrared Spectroscopy and Isotope Labeling. In: Fabian, H., Naumann, D. (eds) Protein Folding and Misfolding. Biological and Medical Physics, Biomedical Engineering. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-22230-6_9
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