Hostname: page-component-586b7cd67f-t8hqh Total loading time: 0 Render date: 2024-11-26T19:07:01.555Z Has data issue: false hasContentIssue false

Synthesis and Application of Gold Nanoparticles Functionalized with Collagen Mimetic Peptides

Published online by Cambridge University Press:  01 February 2011

Xiao Mo
Affiliation:
Department of Materials Science & Engineering, The Johns Hopkins University, Baltimore, MD 21218
Seungju M. Yu
Affiliation:
Department of Materials Science & Engineering, The Johns Hopkins University, Baltimore, MD 21218
Get access

Abstract

Collagen is the principal tensile element of the extra-cellular matrix in animals and is the basic scaffold for cells and tissues. Abnormalities in its structure are known to result in a number of debilitating human diseases. Collagen mimetic peptides (CMPs) with repeat unit of (Pro-Hyp-Gly) are capable of forming right-handed triple-helical structures similar to that of the collagen triple helices. Recently, our group has shown that CMPs exhibit specific binding affinity to natural collagen under controlled thermal conditions. Using solid phase peptide synthesis, we have prepared a CMP cysteine derivative that was used to modify gold nanoparticles. Transmission electron microscopy (TEM) shows that the Cys-CMP functionalized gold nanoparticles have affinity to collagen fibers. We are investigating the interactions between Cys-CMP functionalized gold nanoparticles and collagen fibers. The Cys-CMP conjugated nanoparticles can potentially be used as a tool to visualize and understand unstable domains of collagen fibers which are related to a number of pathological conditions of extra cellular matrices.

Type
Research Article
Copyright
Copyright © Materials Research Society 2005

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCE

1. Holmgren, S. K., Taylor, K. M., Bretscher, L. E. and Raines, R. T., Nature 392, 666 (1998)Google Scholar
2. Tan, W. and Krishnara, R., Desai, T., Tissue Eng. 7, 203, (2001)Google Scholar
3. Pieper, J. S., van Wachem, P. B., van Luyn, M. J. A., Brouser, L. A., Hafmans, T., Veerkamp, J. H. and van Kuppervelt, T. H., Biomaterials 21: 1689 (2001)Google Scholar
4. Wang, Y., Chen, C. and Yu, M. S., submitted (2004)Google Scholar
5. Grabar, K. C., Freeman, R. G., Hommer, M. B. and Natan, M. J., Anal. Chem. 67: 735 (1995)Google Scholar
6. Hayashi, T., Curran-Patel, S. and Prockop, D. J., Biochemistry 18: 4182 (1979)Google Scholar
7. Storhoff, J. J., Elghanian, R., Mucic, R. C., Mirkin, C. A. and Letsinger, R. L., J. Am. Chem. Soc. 120: 1959 (1998)Google Scholar