2022
DOI: 10.1016/j.polymdegradstab.2022.110177
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Role of chlorogenic acid and procyanidin in the modification of self-assembled fibrillar gel prepared from tilapia collagen

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Cited by 10 publications
(4 citation statements)
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“…Finally, QUR, which demonstrated the highest affinity, had a hydrophobic interaction with residue amino acids Pro 65 (3.96 Å), Val 125 (3.25 Å), Ala 129 (3.60 Å) and Leu 203 (3.35 Å), whereas, on the other hand, it has six amino acids of FG (Ser 128, Ser 128, Glu 132, Glu 132, Lys 201 and Ala 204) interacted with hydrogen bonds at distances of 2.56, 2.53, 2.41, 1.82, 2.69 and 2.31 Å. Molecular docking revealed that hydrogen bonding is the main interaction in the ligand–protein interaction, in line with the FTIR analysis. Polyphenols initially interact with protein molecules via hydrophobic interactions and then establish multiple hydrogen bonds 65 . This explains the hydrophobic interactions that occur between all ligands and the protein.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Finally, QUR, which demonstrated the highest affinity, had a hydrophobic interaction with residue amino acids Pro 65 (3.96 Å), Val 125 (3.25 Å), Ala 129 (3.60 Å) and Leu 203 (3.35 Å), whereas, on the other hand, it has six amino acids of FG (Ser 128, Ser 128, Glu 132, Glu 132, Lys 201 and Ala 204) interacted with hydrogen bonds at distances of 2.56, 2.53, 2.41, 1.82, 2.69 and 2.31 Å. Molecular docking revealed that hydrogen bonding is the main interaction in the ligand–protein interaction, in line with the FTIR analysis. Polyphenols initially interact with protein molecules via hydrophobic interactions and then establish multiple hydrogen bonds 65 . This explains the hydrophobic interactions that occur between all ligands and the protein.…”
Section: Resultsmentioning
confidence: 99%
“…Polyphenols initially interact with protein molecules via hydrophobic interactions and then establish multiple hydrogen bonds. 65 This explains the hydrophobic interactions that occur between all ligands and the protein. In addition, the presence of hydrophobic interactions is also very important in terms of increasing emulsion stability.…”
Section: Molecular Simulationmentioning
confidence: 99%
“…The X-ray diffraction (XRD) patterns of CI-TI-s, CI-TI-b, CI-SK-s, and CII-SK-c are shown in Figure 1 l. They reveal the two characteristic peaks in the spectra. the first peak, in the range of 5–10°, was associated with the crystal structure inside the collagen [ 24 ]. The second peak was about 20° at the diffraction angle (2θ), which was associated with diffuse emission from the internal amorphous region of the collagen [ 25 ].…”
Section: Resultsmentioning
confidence: 99%
“…The thermal properties of collagen were determined using differential scanning calorimetry (DSC 3500 Sirius, NETZSCH Scientific Instrument Trading Co., Ltd., Germany) according to Xu et al and An et al The sample (2 mg) was placed in an aluminum crucible and sealed. The sealed empty aluminum crucible was used as a reference.…”
Section: Methodsmentioning
confidence: 99%