The protein secondary structure of native and decellularized samples was studied using Fourier transform infrared spectroscopy (FTIR). NBPs, DBPs, NPPs, and DPPs flaps (10 × 10 mm
2,
n = 3 for each group) were cut and equilibrated for 3–4 h in
deuterium oxide (Janssen, Beerse, Belgium) to reduce the contribution of interfering water bands in the amide-I region [42 (
link)]. FTIR investigations were performed using the
Nicolet iS-50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in the attenuated total reflectance (ATR) mode. The instrument was equipped with a diamond/ZnSe crystal and pressure arm. The transmittance of both samples and background was each measured using 64 scans and infrared spectra were collected within the 4000–500 cm
−1 range, at room temperature. Spectra were then overlapped using a Matlab
® script (Mathworks, Natick, MA, USA) [43 ] to compare the composition of the investigated materials. Amide-I and amide-II bonds, respectively at 1630 cm
−1 and 1550 cm
−1 [40 (
link),43 ], were selected to evaluate the integrity of ECM proteins. Peak transmittance ratio (R) was calculated dividing the intensity of the amide-I peak by the intensity of the amide-II peak.
Todesco M., Imran S.J., Fortunato T.M., Sandrin D., Borile G., Romanato F., Casarin M., Giuggioli G., Conte F., Marchesan M., Gerosa G, & Bagno A. (2022). A New Detergent for the Effective Decellularization of Bovine and Porcine Pericardia. Biomimetics, 7(3), 104.