**4. Conclusions**

*Real Perspective of Fourier Transforms and Current Developments in Superconductivity*

in the 500–4000 cm−1 wave number spectral range with a spectral resolution of 2 cm−1 and 45 scans [18]. The FTIR bone spectrum can be roughly separated into two regions where the organic and inorganic components have distinct peaks (**Figure 5**). The peak at 931.65 cm−1 assigned to the ν1 phosphate band [25–27] is due to the symmetric stretching vibration of the apatitic phosphate ion (PO4

hydroxyapatite [27, 28]. The peak at 1032.92 cm−1 corresponds to the ν3 phosphate

ν3 phosphate peak at 1032.92 cm−1 is coming from the nonstoichiometric hydroxy-

[32]. The peaks at 1235.45 cm−1, 1530.51 cm−1 and 1671.37 cm−1 correspond to the amide group, and they originate from the collagen [27]. The peak at 1235.45 cm−1 corresponds to the amide III results from mixed C-N stretch and N-H in-plane bend with additional contributions from C-Cα stretch [29]. The peak at 1530.51 cm−1 corresponds to the amide II which arises from the combined effect of C-N stretch and N-H in-plane bending [27, 31]. The peak at 1671.37 cm−1 corresponds to the amide I is due to the stretching vibration of the peptide carbonyl group (-C=O) along the polypeptide backbone [27]. The peak at 2879.82 cm−1 is asymmetric CH2 stretch and it arises from the organic component [27]. The peak at 2965.82 cm−1 corresponds to the symmetric CH2 and asymmetric CH3 stretch of the organic component [27]. The peak at 3079.46 cm−1 corresponds to the amide B is due to asymmetric stretching of the CH2 stretching vibration and the absorption due to the CH2 alkyl chain [27]. The weak intensity peak at 3281.99 cm−1 corresponds to the amide A band of collagen is due to N-H stretching vibrations when the N-H group of the peptide is involved in hydrogen bonds [27]. The broad peak at 3536.60 cm−1 is attributed to the pres-

I, amide II and amide III chemical functional groups in the bovine cortical bone

2− decreases, keeping the Ca/(C + P) atomic ratio almost constant

group [27, 33]. The transmittance peaks indicated the presence of

in addition to organic collagen amide A, amide B, amide

band [29, 30] is due to the asymmetric stretching vibration of the PO4

2− or HPO4

apatite which may contain CO3

age, the concentration of CO3

of labile HPO4

ence of the OH<sup>−</sup>

(**Figure 5**).

inorganic ν1, ν3 PO4

3−, OH−

3−) of

3− [27, 31]. The

2− or both in the apatite [27, 31]. With

2− increases during apatite maturation, the amount

*FTIR spectrum of the native cortical bone showing transmittance peaks at 931.65, 1032.92, 1235.45, 1530.51,* 

**44**

**Figure 5.**

*1671.37, 2877.89, 2966.62, 3079.46, 3281.99, 3615 cm−1.*

The FTIR spectra of native and decellularized buffalo aortae, buffalo diaphragms, goat skin, and native bovine cortical bone are presented. The transmittance peaks are that of organic collagen amide A, amide B, amide I, amide II and amide III chemical functional groups in both native and decellularized aortae, diaphragms and skin. In bone, the transmittance peaks are that of inorganic CO3 2−, ν1, ν3 PO4 3−, OH− in addition to organic collagen amide A, amide B, amide I, amide II and amide III chemical functional groups. These important transmittance peaks of the tissue samples will help researchers in defining the chemical structure of these animal tissues.
