Designing the Binding Surface of Proteins to Construct Nano-fibers

Y. Komatsu*, H. Yamada, M. Fukuda, T. Miyakawa, R. Morikawa, M. Takasu, S. Akanuma, A. Yamagishi, S. Kawamoto

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Citations (Scopus)

Abstract

In the field of nanotechnology, a variety of applications have been anticipated. We have been trying to design nano-fibers using proteins while maintaining their native structures. We try to use Lac repressor two-helix protein (LARFH), sulerythrin, and 3-isopropylmalate dehydrogenase (IPMDH) as adaptors for constructing nano-fibers. By making use of the α-helices outside of respective proteins, we are trying to form binding site between proteins: two α-helices of one protein are designed to form four-helix bundle with two α-helices of another protein. In addition, by introducing mutations in amino acids at the binding sites, hydrophobic and electrostatic interactions can be modified. The fiber may be produced upon mixing the two kinds of proteins. By umbrella sampling simulation, we have found that in the combination of LARFH-/-LARFH, hydrophobic interaction is enhanced in wild type, and electrostatic interaction is enhanced in variant. We also found high stability of IPMDH-/-IPMDH.

Original languageEnglish
Title of host publicationProgress in Theoretical Chemistry and Physics
PublisherSpringer Nature
Pages555-567
Number of pages13
DOIs
Publication statusPublished - 2012
Externally publishedYes

Publication series

NameProgress in Theoretical Chemistry and Physics
Volume26
ISSN (Print)1567-7354
ISSN (Electronic)2215-0129

Keywords

  • Electrostatic Interaction
  • Hydrophobic Interaction
  • Molecular Dynamic Simulation
  • Pure Water
  • Umbrella Sampling

ASJC Scopus subject areas

  • Chemistry(all)
  • Physics and Astronomy(all)
  • Biochemistry, Genetics and Molecular Biology (miscellaneous)

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