Hostname: page-component-8448b6f56d-tj2md Total loading time: 0 Render date: 2024-04-24T14:08:32.277Z Has data issue: false hasContentIssue false
  • English
  • Français

Self-Assembly of Proteins into Three-Dimensional Structures Using Bio-Conjugation

Published online by Cambridge University Press:  06 May 2014

Garima Thakur ,
Kovur Prashanthi  and
Thomas Thundat
Garima Thakur
Affiliation:
Department of Chemical and Materials Engineering, University of Alberta, Edmonton, Canada.
Kovur Prashanthi
Affiliation:
Department of Chemical and Materials Engineering, University of Alberta, Edmonton, Canada.
Thomas Thundat
Affiliation:
Department of Chemical and Materials Engineering, University of Alberta, Edmonton, Canada.
Get access

Abstract

Self–assembly of molecular building blocks provides an interesting route to produce well-defined chemical structures. Tailoring the functionalities on the building blocks and controlling the time of self-assembly could control the properties as well as the structure of the resultant patterns. Spontaneous self-assembly of biomolecules can generate bio-interfaces for myriad of potential applications. Here we report self-assembled patterning of human serum albumin (HSA) protein in to ring structures on a polyethylene glycol (PEG) modified gold surface. The structure of the self-assembled protein molecules and kinetics of structure formation entirely revolved around controlling the nucleation of the base layer. The formation of different sizes of ring patterns is attributed to growth conditions of the PEG islands for bio-conjugation. These assemblies might be beneficial in forming structurally ordered architectures of active proteins such as HSA or other globular proteins.

Keywords

biomaterialbiological synthesis (assembly)microstructure
Type
Articles
Information
MRS Online Proceedings Library (OPL) , Volume 1663: Symposium WW – Self-Organization and Nanoscale Pattern Formation , 2014 , mrsf13-1663-ww03-68
Copyright
Copyright © Materials Research Society 2014 

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

REFERENCES

Gates, B. D., Stewart, Q. B.Xu, Ryan, M., D., Willson, C. G., Whitesides, G. M. Chem. Rev. 105, 1171 (2005).10.1021/cr030076oCrossRefGoogle Scholar
Dri, C., Peters, M. V., Schwarz, J., Hecht, S., Grill, L. Nature Nanotech. 3, 649 (2008).10.1038/nnano.2008.269CrossRefGoogle Scholar
Chen, C.-L., Keith, M. B., Oradian-Odak, J., James, J. D. J. Am. Chem. Soc. 133, 17406 (2011).10.1021/ja206849cCrossRefGoogle Scholar
Singh, G., Griesser, H. J., Bremmell, K., Kingshott, P., Adv. Funct. Mater. 21, 540 (2011).10.1002/adfm.201001340CrossRefGoogle Scholar
Zhou, Y., Huang, W., Liu, J., Zhu, X., Yan, D., Adv. Mater. 22, 4567–4590 (2010).10.1002/adma.201000369CrossRefGoogle Scholar
Jeyachandran, Y. L., Zharnikov, M., J. Phys. Chem. C, 116, 4950 (2012).Google Scholar
Thakur, G., Prashanthi, K., Thundat, T. Sci. Rep 3. doi:10.1038/srep01923 (2013).Google Scholar
Rundqvist, J., Hoh, J. H., , D. Haviland, B. Langmuir, 21, 2981 (2005).10.1021/la0471792CrossRefGoogle Scholar
Pribie, R., VanStokkum, I. H. M., Chapman, D., Haris, P. I., Bolemendal, M. Anal. Biochem. 214, 366 (1993).10.1006/abio.1993.1511CrossRefGoogle Scholar