Surface Characterization of Insulin Protofilaments and Fibril Polymorphs Using Tip- Enhanced Raman Spectroscopy (TERS) Dmitry Kurouski, Tanja Deckert-Gaudig,

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Presentation transcript:

Surface Characterization of Insulin Protofilaments and Fibril Polymorphs Using Tip- Enhanced Raman Spectroscopy (TERS) Dmitry Kurouski, Tanja Deckert-Gaudig, Volker Deckert, Igor K. Lednev Biophysical Journal Volume 106, Issue 1, Pages 263-271 (January 2014) DOI: 10.1016/j.bpj.2013.10.040 Copyright © 2014 Biophysical Society Terms and Conditions

Figure 1 SEM images of twisted (a) and flat (b) insulin fibrils. Scale bar is 100 nm. Biophysical Journal 2014 106, 263-271DOI: (10.1016/j.bpj.2013.10.040) Copyright © 2014 Biophysical Society Terms and Conditions

Figure 2 Selected TERS spectra acquired from the surfaces of insulin fibril polymorphs and their protofilaments. TERS spectra collected from the surfaces of twisted (—) and flat (····) fibrils as well as their protofilaments (—). Specific amino acid vibrational modes are marked with gray lines. Amide I bands are marked with dashed lines, showing the borders between protein secondary structures. NH2/NH3+ (1144 cm−1) and COOH/COO− (1687–1700 cm−1) vibrational modes are also indicated. Biophysical Journal 2014 106, 263-271DOI: (10.1016/j.bpj.2013.10.040) Copyright © 2014 Biophysical Society Terms and Conditions

Figure 3 Amino acids and charged chemical groups have different frequency presence on the surface of twisted and flat fibril polymorphs as well as their protofilaments. Relative frequency plot of amino acid residues on the surfaces of twisted fibrils (black), flat fibrils (grey), and their protofilaments (white) obtained based on acquired TERS spectra. To obtain the relative frequency, the number of spectra containing a specific amino acid residue was divided by the total number of TERS or SERS spectra in each group. The resulting value was then multiplied by 100 to obtain a percentage. To see this figure in color, go online. Biophysical Journal 2014 106, 263-271DOI: (10.1016/j.bpj.2013.10.040) Copyright © 2014 Biophysical Society Terms and Conditions

Figure 4 Insulin fibril polymorphs and their protofilaments have different composition of protein secondary structures on their surfaces. Relative frequencies of protein secondary structures of the surface of flat and twisted fibril polymorphs as well as their protofilaments: α-helix/unordered (black), β-sheet (gray), and a mixture of β-sheet, α-helical, and unordered (white). Biophysical Journal 2014 106, 263-271DOI: (10.1016/j.bpj.2013.10.040) Copyright © 2014 Biophysical Society Terms and Conditions

Scheme 1 A model of carboxyl group integration in the protofilaments’ propagation. COOH-rich areas (red) of two protofilaments lead to their association and twisted fibril formation. Biophysical Journal 2014 106, 263-271DOI: (10.1016/j.bpj.2013.10.040) Copyright © 2014 Biophysical Society Terms and Conditions

Scheme 2 Model of flat (a) and twisted (b) fibril formation. Protofilaments associate side-by-side forming Tape fibrils. Alternatively, surface-driven templating by β-sheet-rich clusters (shown in red) leads to the formation of twisted fibrils. Biophysical Journal 2014 106, 263-271DOI: (10.1016/j.bpj.2013.10.040) Copyright © 2014 Biophysical Society Terms and Conditions