Agen are shown in of collagen [23]. The UV absorption spectra of lizardfish scales collagen are shown in Fig C2 Ceramide web molecular chains [28]. The distance in between the molecular chains of PSC was higher than Figure 2a, namely, ASC and PSC showed sharp and intense maximum absorption peaks at ure 2a, namely, ASC and PSC showed sharp and intense maximum absorption peaks at that inside ASC, indicating weaker molecular interactions in PSC. This may possibly be related to 235 nm and 236 nm, respectively, which is consistent with the UV absorption characteristics 235 nm and 236 nm, respectively, which can be constant together with the UV absorption characteris the cleavage in the terminal peptide sequence of collagen [29]. The d worth with the second of type I collagen [25]. The aromatic residues, including tyrosine and phenylalanine, have tics of type I collagen [25]. The aromatic residues, like tyrosine and phenylalanine, comparatively broad peak of ASC was 4.18 and that of PSC was four.23 and this reflects the a maximum absorption peak at 280 nm. As shown in Figure 2a, ASC and PSC did not have a maximum absorption peak at 280 nm. As shown in Figure 2a, ASC and PSC did distance involving their skeletons [22]. peak at 280 nm. demonstrate a substantial absorption not demonstrate a Ethyl Vanillate Epigenetic Reader Domain significant absorption peak at 280 nm.2.3.2. FourierTransform Infrared (FTIR) Spectrum FTIR spectra of collagen from lizardfish scales are displayed in Figure 2b. ASC and PSC from lizardfish scales contained five major characteristic absorption bands, like Amide A, Amide B, Amide I, Amide II, and Amide III. The Amide A band (3400440 cm-1) is primarily associated with all the stretching vibration of N [18]. Having said that, the hydro gen bond formation leads to a adjust in wavenumber to a lower frequency [18]. The Am ide A absorption bands of ASC and PSC have been located at 3307 cm-1 and 3324 cm-1, respec tively, indicating that N groups had been involved in the formation of hydrogen bonds, which resulted in a shift of your Amide A band towards the reduce frequency. The Amide B band (a) (b) (3080 cm-1) is linked for the asymmetrical stretch of H2. We showed that the Amide B bands of ASC and PSC were situated at 3080 cm-1. Inside the present study, the positions of Amide I bands of ASC and PSC had been located at wavenumbers of 1653 cm-1 and 1654 cm-1, respectively; Amide II bands of each ASC and PSC were situated at 1542 cm-1; and Amide III bands of ASC and PSC have been observed at 1240 cm-1 and 1241 cm-1, respectively. Extra over, the ratios of absorption intensities involving the Amide III band and 1450 cm-1 band had been about 1.0, confirming that the triple helical structures of ASC and PSC were effectively maintained [6]. (c) (d)Figure two. Spectroscopy properties of ASC and PSC. (a) UV absorption spectra, (b) Fourier transform Figure two. Spectroscopy properties of ASC and PSC. (a) UV absorption spectra, (b) Fourier transform infrared spectroscopy, (c) circular dichroism, and (d) Xray diffraction. The experiment was con infrared spectroscopy, (c) circular dichroism, and (d) X-ray diffraction. The experiment was performed ducted only once (n = 1) only as soon as (n = 1).2.3.2. Fourier-Transform Infrared (FTIR) Spectrum FTIR spectra of collagen from lizardfish scales are displayed in Figure 2b. ASC and PSC from lizardfish scales contained five major characteristic absorption bands, includingMar. Drugs 2021, 19,4 ofAmide A, Amide B, Amide I, Amide II, and Amide III. The Amide A band (3400440 cm-1 ) is mostly associa.
