Journal
ACS BIOMATERIALS SCIENCE & ENGINEERING
Volume 5, Issue 9, Pages 4272-4284Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsbiomaterials.9b00593
Keywords
polyphenol; tannic acid; epigallocatechin gallate; N-2-(3,4-dihydroxylphenyl) ethyl acrylamide; collagen; cross-linking
Categories
Funding
- National Natural Science Foundation of China, China [81571018]
- key programs for science and technology development of the Anhui province, China [1804h08020232]
- department of science and technology, Hefei, China [YW201710120001]
- Fund of the Board of Education of Anhui Province [gxbjZD2016033]
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This study is aimed to investigate the relationship of the mechanism and the effect of polyphenol derivatives cross-linking collagen with polyphenol molecular structural complexity and reaction conditions of polyphenols with collagen and to present a reference for cross-linker selection. Three kinds of polyphenols were selected to cross-link collagen under nonoxidized and oxidized conditions in vitro. These polyphenols included tannic acid, which represents the most complex stereo structure and the highest number of phenolic hydroxyl groups; epigallocatechin gallate, which represents a moderately complex structure and contains fewer phenolic hydroxyl groups than tannic acid; and N-2-(3,4-Collagen Triple-htlix dihydroxylphenyl) ethyl acrylamide, which represents only one hydroxyl phenol group. Particle size analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, attenuated total reflection Fourier transform infrared spectroscopy, and cross-linking degree analysis were conducted. Mechanical properties thermal stability, swelling properties, hydrophilicity, and antienzymolysis properties were also determined. Results showed that all polyphenol derivatives cross-linked collagen mainly by noncovalent bonding under acidic nonoxidized conditions and by covalent bonding under alkaline-oxidized conditions. In general, the modification effect of polyphenol on collagen was related to its molecular complexity and the number of its phenolic hydroxyls. Several phenolic hydroxyls in the polyphenol derivative caused a good modification effect on collagen, especially under acidic nonoxidized conditions. Under alkaline conditions, each polyphenol was oxidized, resulting in improved cross-linking strength by covalent bonding compared to that under acidic nonoxidized condition via noncovalent bonding. The selection of cross-linkers and cross-linking conditions should be based on the purpose of collagen modification consistent with the effect of cross-linking.
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