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Atomic Force Microscopic Study of Morphological Changes for Treated and Untreated Collagen Fibers of Mongolian Goatskins

Published online by Cambridge University Press:  21 March 2011

Enkhbaatar Ankhbayar
Affiliation:
Center for Nanoscience and Nanotechnology and Department of Chemical Technology, School of Chemistry and Chemical Engineering, National University of Mongolia, Ulaanbaatar, Mongolia
Byamba Itgel
Affiliation:
School of Biological Resource and Management, Mongolian State University of Agriculture, Ulaanbaatar, Mongolia
Byambadembrel Batkhuu
Affiliation:
Center for Nanoscience and Nanotechnology and Department of Chemical Technology, School of Chemistry and Chemical Engineering, National University of Mongolia, Ulaanbaatar, Mongolia
Dashnyam Urnaa
Affiliation:
Research and Experimental Center of the ARMONO, Ulaanbaatar, Mongolia
Chimed Ganzorig
Affiliation:
Center for Nanoscience and Nanotechnology and Department of Chemical Technology, School of Chemistry and Chemical Engineering, National University of Mongolia, Ulaanbaatar, Mongolia
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Abstract

In this study, the morphological changes of chemically treated (or preserved) with aqueous solutions of 1) a sodium chloride (NaCl) and 2) a compound containing sodium silicate, so called “wasserglass”, and untreated I-type collagen fibers of Mongolian goatskin are investigated by atomic force microscopy in ambient condition and at room temperature. The experimental results show that the difference between D period for both chemically treated and untreated collagen fibers are a relatively stable for morphological behavior. However, we find that the width of collagen fibers treated with the NaCl solution is more increasing with approximately 112 nm than those of samples (untreated and treated with wasserglass solution) for the range 93.4-94.8 nm. We also observe that a typically structure of the collagen fibers generally, a dense packing of the untreated and treated by wasserglass collagen fibers in bundles in a nearly parallel arrangement, with little changes in orientation can be seen. The collagen fibers treated by NaCl are a more destructive than untreated and treated by wasserglass for collagen fibers.

Type
Research Article
Copyright
Copyright © Materials Research Society 2011

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References

REFERENCES

1. Soluble Silicates in Leather Production 2003. Available from: www.leathermag.com. Accessed July 10, 2010.Google Scholar
2. Javkhlantugs, N., Ankhbayar, E., Tegshjargal, Kh., Enkhjargal, D., and Ganzorig, C., Mater. Sci. Forum 610, 175 (2009).10.4028/www.scientific.net/MSF.610-613.175Google Scholar
3. Di LulloDagger, G. A., Sweeney, S. M., Kőrkkő, J., Ala-Kokko, Leena, and San Antonio, J. D., J. Biol. Chem. 277, 4223 (2002).Google Scholar
4. Stefan, S., Albert, Z., Marek, J., Wolfgang, H., and Stefan, T., Biochem. Biophys. Res. Commun. 354, 27 (2007).Google Scholar
5. Schmitt, F. D., Hall, C. E., and Jakns, M. A., J. Cell. Comp. Physiol. 20, 11 (1942).Google Scholar
6. Chapman, J. A., and Hulmes, D. J. S., “Electron microscopy of the collagen fibril”, in Ultrastructure of the Connective Tissue Matrix, edited by. Motta, P. M., and Ruggeri, A., (Kluwer Academic Publishers, 1984) pp. 133.Google Scholar
7. Baselt, D. R., Revel, J. P., and Baldeschwieler, J. D., Biophys. J. 65, 2644 (1993).Google Scholar
8. Revenko, I., Sommer, F., Minh, D. T., Garrone, R., and Franc, J. M., Biol. Cell 80, 67 (1994).Google Scholar
9. Venturoni, M., Gutsmann, T., Fantner, G. T., Kindt, J. H., and Hansma, P. K., Biochem. Biophys. Res. Commun. 303, 508 (2003).Google Scholar
10. Ramachandra, G. N., and Karthan, G., Nature (London) 176, 593 (1955).Google Scholar
11. Kadler, K. E., Holmes, D. F., Trotter, J. A., and Chapman, J. A., Biochem. J. 316, 1 (1996).Google Scholar
12. Tadayuki, N., Fumio, N., and Keiji, K., J. Fac. Appl. Biol. Sci. 30, 103 (1991).Google Scholar
13. Binnig, G., Quate, C., and Gerber, C., Phys. Rev. Lett. 56, 930 (1986).Google Scholar
14. Lin, A.C., and Goh, M.C., Proteins 49 378 (2002).Google Scholar
15. Ankhbayar, E., Itgel, B., Batkhuu, B., and Ganzorig, C., 2010 (unpublished).Google Scholar