期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 48, 期 2, 页码 354-359出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2010.12.012
关键词
Collagen; Procyanidin; Modification
资金
- National Natural Science Foundation (NNSF) of China [20704028, 21074074]
- Science and Technology Planning Project of Sichuan Province [2010HH0004]
- Ministry of Education of China [20090181110061]
We have investigated the modification of collagen with a natural plant polyphenol, procyanidin under acidic conditions. Fourier transform infrared spectroscopy (FTIR) and Atomic force microscopy (AFM) studies demonstrate that the hydrogen bond interactions between collagen and procyanidin does not destroy the triple helix conformation of collagen, and the fibril aggregation occurs because of the cross-linking with procyanidin. The water contact angle (WCA) tests indicate that the hydrophobicity of the procyanidin modified collagen films can be improved. Whereas, the water vapor permeability (WVP) of the films decrease with the increasing procyanidin content due to the formation of denser structure. Moreover, differential scanning calorimetry (DSC) and thermogravimetric (TG) measurements reveal that the collagen/procyanidin films have improved thermal stability in comparison with pure collagen. The present study reveals that procyanidin stabilizes collagen as a cross-linker and preserves its triple helical structure.
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