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Polypeptide-Solvent Interactions Measured by Single Molecule Force Spectroscopy

Published online by Cambridge University Press:  26 February 2011

Alexei Valiaev ,
Dong Woo Lim ,
Ashutosh Chilkoti ,
Scott Schmidler  and
Stefan Zauscher
Alexei Valiaev
Affiliation:
av12@duke.edu, Duke University, Mechanical Engineering and Materials Science, United States
Dong Woo Lim
Affiliation:
dong.lim@duke.edu, Duke University, Biomedical Engineering, United States
Ashutosh Chilkoti
Affiliation:
chilkoti@duke.edu, Duke University, Biomedical Engineering, United States
Scott Schmidler
Affiliation:
schmidler@stat.duke.edu, Duke University, Institute of Statistics and Decision Sciences, United States
Stefan Zauscher
Affiliation:
zauscher@duke.edu, Duke University, Mechanical Engineering and Materials Science, United States
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Abstract

Stimulus-responsive biomolecules have attracted a large research interest because of their potential application in various areas such as drug delivery, actuators and sensing devices at the nanoscale. Using single-molecule force spectroscopy (SMFS) we studied elastin-like polypeptides (ELPs). These stimulus-responsive polypeptides undergo an inverse temperature transition, accompanied by a large conformational change, when the solvent quality is changed by increasing the temperature or by addition of salt. Understanding the relationship between peptide sequence and mechanisms of force generation can provide a route to engineer ELPs with desirable mechano-chemical properties. Here we studied the effect of solvent quality and type of guest residue on the mechanical properties of ELPs on the single-molecule level. We used a statistical approach to estimate polymer elasticity parameters from model fits to the data. With this approach we were able to resolve small changes in the Kuhn segment length distributions associated with different molecular architectures. We then show that these mechanical differences likely arise from differences in the hydrophobic hydration of sidegoups, in line with recent predictions from molecular dynamics simulations.

Keywords

elastic propertiesscanning probe microscopy (SPM)microstructure
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 898: Symposium L – Mechanical Behavior of Biological and Biomimetic Materials , 2005 , 0898-L06-06-NN04-06
Copyright
Copyright © Materials Research Society 2006

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References

1. Janshoff, A., Neitzert, M., Oberdorfer, Y., and Fuchs, H., Angewandte Chemie-International Edition 39, 3213 (2000).Google Scholar
2. Zhang, W., and Zhang, X., Progress in Polymer Science, 28, 1271 (2003).Google Scholar
3. Urry, D.W.,, Journal of Physical Chemistry B 101, 11007 (1997).Google Scholar
4. Li, B., Alonso, D.O.V., Bennion, B. J. and Daggett, V., Journal of the American Chemical Society 123, 11991 (2001).Google Scholar
5. Meyer, D.E., and Chilkoti, A., Nature Biotechnology 17, 1112 (1999).Google Scholar
6. Mardia, K.V., and Jupp, P.E., Directional statistics. (John Wiley & Sons, New York, 2000).Google Scholar
7. Luan, C.H., Harris, R. D., Prasad, K. U., and Urry, D. W., Biopolymers 29, 1699 (1990).Google Scholar
8. Gosline, J.M., Yew, F.F., and Weis-Fogh, T., Biopolymers 14, 1811 (1975).Google Scholar
9. Li, B., Alonso, D.O.V., and Daggett, V., Journal of Molecular Biology 305, 581 (2001).Google Scholar