1979
DOI: 10.1016/0022-2836(79)90438-8
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Glutaraldehyde-induced states of stress of the collagen triple helix

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1980
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Cited by 14 publications
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“…After cross-linking with glutaraldehyde, the amide I peaks positions shifted to 1642.6 cm − 1 and the reduced intensity indicates the conformational change in triple helix. 30 32 The amide II peak position also shifted towards higher wavenumber from 1554.26 to 1571.78 cm − 1 and increased intensity, indicating that amino (-NH 2 ) groups of the lysine residue of collagen react with aldehyde (-CHO) groups of glutaraldehyde to form the aldimine linkage (CH=N). 33 The peaks at 1452.67 cm − 1 disappeared and 1410.18 cm − 1 transformed into an intense peak suggesting an increase in symmetric CH 3 bending vibration.…”
Section: Resultsmentioning
confidence: 99%
“…After cross-linking with glutaraldehyde, the amide I peaks positions shifted to 1642.6 cm − 1 and the reduced intensity indicates the conformational change in triple helix. 30 32 The amide II peak position also shifted towards higher wavenumber from 1554.26 to 1571.78 cm − 1 and increased intensity, indicating that amino (-NH 2 ) groups of the lysine residue of collagen react with aldehyde (-CHO) groups of glutaraldehyde to form the aldimine linkage (CH=N). 33 The peaks at 1452.67 cm − 1 disappeared and 1410.18 cm − 1 transformed into an intense peak suggesting an increase in symmetric CH 3 bending vibration.…”
Section: Resultsmentioning
confidence: 99%