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Stability of Chemically Crosslinked Microtubules

Published online by Cambridge University Press:  15 March 2011

Andrew K. Boal ,
Susan B. Rivera ,
Nicholas E. Miller ,
George D. Bachand  and
Bruce C. Bunker
Andrew K. Boal
Affiliation:
Biomolecular Materials and Interfaces, MS1413 Sandia National Laboratory PO Box 5800 Albuquerque, NM 87123, USA
Susan B. Rivera
Affiliation:
Biomolecular Materials and Interfaces, MS1413 Sandia National Laboratory PO Box 5800 Albuquerque, NM 87123, USA
Nicholas E. Miller
Affiliation:
Biomolecular Materials and Interfaces, MS1413 Sandia National Laboratory PO Box 5800 Albuquerque, NM 87123, USA
George D. Bachand
Affiliation:
Biomolecular Materials and Interfaces, MS1413 Sandia National Laboratory PO Box 5800 Albuquerque, NM 87123, USA
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Abstract

Microtubules (MT) are dynamic protein-based polymers with numerous applications in materials science including the active transport of nanomaterials and as templates for biomimetic materials synthesis. Some of these applications require that the dynamic nature of the MT be suppressed, and in this report we will discuss the preparation and stability of chemically crosslinked microtubules (CLMTs). MT reaction with gluteraldehyde results in the formation of protein dimers and higher molecular weight oligimers as observed by gel electrophoresis, confirming the formation of covalent inter-protein linkages. While extensive crosslinking was found to destabilize MTs and inactivate them with regards to kinesin binding, moderate amounts of crosslinking lead to CLMTs that had functional lifetimes of at least twice that of uncrosslinked MTs. Further studies demonstrated that CLMTs exhibited a wider thermal stability window and were far more resistant to metal-ion induced depolymerization than uncrosslinked MTs.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 826: Symposium V – Proteins as Materials , 2004 , V3.1
Copyright
Copyright © Materials Research Society 2004

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