Biomedical Engineering Reference
In-Depth Information
The derivative peaks obtained from TGA for all the experimental samples at opti-
mized concentration (1.5% of AA) were illustrated in Figure 4(a) and 4(b). In Figure
(a) and (b) maximum weight loss of AA was observed at 252°C and for Type I and
Type III collagen it was 327°C whereas in AACC 1 and AACC 3 it was observed at
345 and 370°C respectively. When AA were cross-linked with Type I and Type III
collagen at different concentrations, thermal stability increases as the percentage of
AA increased up to 1.5%. Further increase in AA reduces the thermal stability of the
resulting material.
Figure 4. (a) and 4(b) in maximum weight loss of AA was observed at 252°C and for Type I and Type
III collagen
table 1. Tensile strength measurements of Type I, Type III collagen, AACC 1and AACC 3 by Universal
Testing Machine (INSTRON model 1405) at a crosshead speed of 5mm/min.
Material Type
Tensile Strength (MPa)
Young's modulus (Gpa)
Elongation at break (%)
Type I collagen
Type III collagen
2.110
2.10
7.8
7.3
31.99
30.89
AACC 1
11.56
47.08
5.31
AACC 3
10.73
45.12
5.21
With regard to mechanical property, about 5 to 6-fold increase in tensile strength
was observed after cross-linking with AA. The tensile strength measurements of na-
tive, AACC 1 and AACC 3 were taken and the ultimate tensile strength (MPa) and
Young's modulus (Gpa) values were represented in Table 1.
iNtermoleCular h-BoNd iNteraCtioN BetWeeN tyPe i, tyPe
iii CollaGeN aNd aa By BiNdiNG eNerGy CalCulatioN usiNG
BioiNFormatiCs tool soFtWare
For binding energy and bonding pattern assessment, docking study was followed.
For the docking study, chemical structures were generated using ACD/ChemSketch
(ACD/ChemSketch Version 12 Advanced Chemistry Development, Inc., Toronto, ON,
Canada. 2009.). The 3D structure of collagen was generated using gencollagen pro-
gram (http://www.cgl.ucsf.edu./cgi-bin/gencollagen.py). To find out the interaction
 
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