2010
DOI: 10.1016/j.ecoenv.2009.12.005
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UV–vis and FT-IR spectra of ultraviolet irradiated collagen in the presence of antioxidant ascorbic acid

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Cited by 67 publications
(39 citation statements)
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“…Collagen amino acids possess endogenous chromophoric sites (aromatic residues) such as tyrosine and phenylalanine which absorb the UV radiations in the range of 250-300 nm [12,[25][26][27]. The energetic UV radiations initiate photodegradation of these aromatic amino acids to form crosslinks called dityrosine [12,17,26,28,29]. This enhances the hardness and stiffness which increases the E 0 [12,30].…”
Section: Resultsmentioning
confidence: 97%
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“…Collagen amino acids possess endogenous chromophoric sites (aromatic residues) such as tyrosine and phenylalanine which absorb the UV radiations in the range of 250-300 nm [12,[25][26][27]. The energetic UV radiations initiate photodegradation of these aromatic amino acids to form crosslinks called dityrosine [12,17,26,28,29]. This enhances the hardness and stiffness which increases the E 0 [12,30].…”
Section: Resultsmentioning
confidence: 97%
“…The energetic UV radiations initiate photodegradation of these aromatic amino acids to form crosslinks called dityrosine [12,17,26,28,29]. This enhances the hardness and stiffness which increases the E 0 [12,30]. Further absorption of the UV radiation forms new photoproducts such as pentosidine and pyridinoline that add more crosslinks [9,16].…”
Section: Resultsmentioning
confidence: 99%
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“…In the UV region, the peak at 200 nm indicates peptide absorption peak in protein, whereas a second weak absorption peak at about 278 nm is due to aromatic amino acids 43,44 . Aggregation in the protein structure may lead to the decrease in absorbance values indicating the strong interaction.…”
Section: Uv-vis Spectroscopic Studiesmentioning
confidence: 99%