Nanoscale characterization of acid and thermally treated collagen fibrils.
Type I collagen is a major extracellular matrix component and its hierarchical structure plays an essential role in the regulation of cellular behavior. Here, we have analyzed the changes in the morphological, chemical, and mechanical properties of collagen fibrils induced by acidic and thermal treatments and the influence on the cellular response of MC3T3-E1 cells. Morphological changes induced by the disintegration of the fibrillar structure of collagen were observed using atomic force microscopy. The changes in the surface chemistry due to the disassembly of native collagen fibrils were observed using time-of-flight secondary ion mass spectroscopy (ToF-SIMS). ToF-SIMS spectra were very sensitive to changes in the molecular configuration of the collagen fibrils induced by acidic and thermal treatments due to the extreme surface specificity. In addition, ToF-SIMS showed clear and reproducible changes in the surface amino acid composition corresponding to the acidic and thermal treatments of collagen fibrils. Based on the quantitative map of surface elastic modulus measured by contact-resonance force microscopy, acid and thermally treated collagen showed a lower elastic modulus than native collagen fibrils. Compared with native collagen fibrils, reduced cell spreading and decreased viability of MC3T3-E1 cells were observed on both the acid and thermally treated collagen.
Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), 335 Science Rd., Daejeon 305-701, Republic of Korea.
Young Jae
YJ
Park
Gyu Jin
GJ
Choi
Se-Hwa
SH
Kim
Junhee
J
Hahn
Tae Geol
TG
Lee
Won Jong
WJ
Lee
Dae Won
DW
Moon
D016475:3T3 Cells; D000143:Acids / Q000737:chemistry*; D000818:Animals; D003094:Collagen / Q000737:chemistry*; D051379:Mice; D018625:Microscopy, Atomic Force; D036103:Nanotechnology
D000143:Acids; D003094:Collagen