| 000 | 02847nam a2200277Ia 4500 | ||
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| 003 | MX-MdCICY | ||
| 005 | 20250625162428.0 | ||
| 040 | _cCICY | ||
| 090 | _aB-19307 | ||
| 245 | 1 | 0 | _aTwo-dimensional infrared spectroscopic study on the thermally induced structural changes of glutaraldehyde-crosslinked collagen |
| 490 | 0 | _vSpectrochimica Acta Part A: Molecular and BioMolecular Spectroscopy, 140, p.356-363, 2015 | |
| 520 | 3 | _aThe thermal stability of collagen solution (5 mg/mL)crosslinked by glutaraldehyde (GTA)[GTA/collagen (w/w)= 0.5]was measured by differential scanning calorimetry and Fourier transform infrared spectroscopy (FTIR), and the thermally induced structural changes were analyzed using two-dimensional (2D)correlation spectra. The denaturation temperature (Td)and enthalpy change (?H)of crosslinked collagen were respectively about 27 °C and 88 J/g higher than those of native collagen, illuminating the thermal stability increased. With the increase of temperature, the red-shift of absorption bands and the decreased AIII/A1455 value obtained from FTIR spectra indicated that hydrogen bonds were weakened and the unwinding of triple helix occurred for both native and crosslinked collagens; whereas the less changes in red-shifting and AIII/A1455 values for crosslinked collagen also confirmed the increase in thermal stability. Additionally, the 2D correlation analysis provided information about the thermally induced structural changes. In the 2D synchronous spectra, the intensities of auto-peaks at 1655 and 1555 cm?1, respectively assigned to amide I band (Cdouble bondO stretching vibration)and amide II band (combination of Nsingle bondH bending and Csingle bondN stretching vibrations)in helical conformation were weaker for crosslinked collagen than those for native collagen, indicating that the helical structure of crosslinked collagen was less sensitive to temperature. Moreover, the sequence of the band intensity variations showed that the band at 1555 cm?1 moved backwards owing to the addition of GTA, demonstrating that the response of helical structure of crosslinked collagen to the increased temperature lagged. It was speculated that the stabilization of collagen by GTA was due to the reinforcement of triple helical structure. | |
| 650 | 1 | 4 | _aCOLLAGEN |
| 650 | 1 | 4 | _aGLUTARALDEHYDE |
| 650 | 1 | 4 | _aDIFFERENTIAL SCANNING CALORIMETRY |
| 650 | 1 | 4 | _aFOURIER TRANSFORM INFRARED SPECTROSCOPY |
| 650 | 1 | 4 | _aTWO-DIMENSIONAL CORRELATION ANALYSIS |
| 700 | 1 | 2 | _aTian, Z. |
| 700 | 1 | 2 | _aWu, K. |
| 700 | 1 | 2 | _aLiu, W. |
| 700 | 1 | 2 | _aShen, L. |
| 700 | 1 | 2 | _aLi, G. |
| 856 | 4 | 0 |
_uhttps://drive.google.com/file/d/1gsrd5yzKUpgGhE4MO0B0trzJDXU6PJwI/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
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