Abstract
Fourier transform infrared (FTIR) spectroscopy provides data that are widely used for secondary structure characterization of peptides. A wide array of available sampling methods permits structural analysis of peptides in diverse environments such as aqueous solution (including optically turbid media), powders, detergent micelles, and lipid bilayers. In some cases, side chain vibrations can also be resolved and used for tertiary structure and chemical analysis. Data from several low-resolution spectroscopic techniques, including FTIR, can be combined to generate an empirical phase diagram, an overall picture of peptide structure as a function of environmental conditions that can aid in the global interpretation of large amounts of spectroscopic data.
Kunal Bakshi and Mangala R. Liyanage have contributed equally to this chapter.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Venyaminov SY, Kanin NN (1990) Quantitative IR spectrophotometery of peptide compounds in water (H2O) solutions. Spectral parameters of amino acid residue absorption bands. Biopolymers 30:1243–1257
Surewicz WK, Mantsch HH, Chapman D (1993) Determination of protein secondary structure by Fourier transform infrared. Biochemistry 32:389–394
Vass E, Hollósi M, Besson F, Buchet R (2003) Vibrational spectroscopic detection of beta and gamma turns in synthetic and natural peptides and proteins. Chem Rev 103:1917–1954
Ganim Z, Chung HS, Smith AW, Deflores LP, Jones KC, Tokmakoff A (2008) Amide I two-dimensional infrared spectroscopy of proteins. Acc Chem Res 41(3):432–441
Van de Weert M, Haris PI, Hennink WE, Crommelin DJA (2001) Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Anal Biochem 297(2):160–169
Fan H, Ralston J, Dibiase M, Faulkner E, Middaugh CR (2005) Solution behavior of IFN-beta-1a: an empirical phase diagram based approach. J Pharm Sci 94:1893–1911
Kueltzo LA, Ersoy B, Ralston JP, Middaugh CR (2003) Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: a bGCSF case study. J Pharm Sci 92:1805–1820
Nonoyama A, Laurence JS, Garriques L, Qi H, Le T, Middaugh CR (2008) A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams. J Pharm Sci 97(7):2552–2567
Maddux NR, Joshi SB, Volkin DB, Ralston JP, Middaugh CR (2011) Multidimensional methods for the formulation of biopharmaceuticals and vaccines. J Pharm Sci 100(10):4171–4197
Maddux NR, Rosen IT, Hu L, Olsen CM, Volkin DB, Middaugh CR (2012) An improved methodology for multidimensional high-throughput preformulation characterization of protein conformational stability. J Pharm Sci 101(6):2017–2024
Kim JH, Iyer V, Joshi SB, Volkin DB, Middaugh CR (2012) Improved data visualization techniques for analyzing macromolecule structural changes. Protein Sci 21(10):1540–1553
Iyer V, Maddux N, Hu L, Cheng W, Youssef AK, Winter G, Joshi SB, Volkin DB, Middaugh CR (2013) Comparative signature diagrams to evaluate biophysical data for differences in protein structure across various formulations. J Pharm Sci 102(1):43–51
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Bakshi, K., Liyanage, M.R., Volkin, D.B., Middaugh, C.R. (2014). Fourier Transform Infrared Spectroscopy of Peptides. In: Nixon, A. (eds) Therapeutic Peptides. Methods in Molecular Biology, vol 1088. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-673-3_18
Download citation
DOI: https://doi.org/10.1007/978-1-62703-673-3_18
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-672-6
Online ISBN: 978-1-62703-673-3
eBook Packages: Springer Protocols