Speeding up biomolecular interactions by molecular sledding
Abstract
In numerous biological processes associations involve a protein with its binding partner, an event that is preceded by a diffusion-mediated search bringing the two partners together. Often hindered by crowding in biologically relevant environments, three-dimensional diffusion can be slow and result in long bimolecular association times. Moreover, the initial association step between two binding partners often represents a rate-limiting step in biotechnologically relevant reactions. We also demonstrate the practical use of an 11-a.a. DNA-interacting peptide derived from adenovirus to reduce the dimensionality of diffusional search processes and speed up associations between biological macromolecules. We functionalize binding partners with the peptide and demonstrate that the ability of the peptide to one-dimensionally diffuse along DNA results in a 20-fold reduction in reaction time. We also show that modifying PCR primers with the peptide sled enables significant acceleration of standard PCR reactions.
- Authors:
-
- Univ. of Groningen (Netherlands)
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Publication Date:
- Research Org.:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- OSTI Identifier:
- 1260167
- Report Number(s):
- BNL-112327-2016-JA
Journal ID: ISSN 2041-6520; CSHCBM
- Grant/Contract Number:
- SC00112704
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Chemical Science
- Additional Journal Information:
- Journal Volume: 7; Journal Issue: 2; Journal ID: ISSN 2041-6520
- Publisher:
- Royal Society of Chemistry
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Turkin, Alexander, Zhang, Lei, Marcozzi, Alessio, Mangel, Walter F., Herrmann, Andreas, and van Oijen, Antoine M. Speeding up biomolecular interactions by molecular sledding. United States: N. p., 2015.
Web. doi:10.1039/C5SC03063C.
Turkin, Alexander, Zhang, Lei, Marcozzi, Alessio, Mangel, Walter F., Herrmann, Andreas, & van Oijen, Antoine M. Speeding up biomolecular interactions by molecular sledding. United States. https://doi.org/10.1039/C5SC03063C
Turkin, Alexander, Zhang, Lei, Marcozzi, Alessio, Mangel, Walter F., Herrmann, Andreas, and van Oijen, Antoine M. Wed .
"Speeding up biomolecular interactions by molecular sledding". United States. https://doi.org/10.1039/C5SC03063C. https://www.osti.gov/servlets/purl/1260167.
@article{osti_1260167,
title = {Speeding up biomolecular interactions by molecular sledding},
author = {Turkin, Alexander and Zhang, Lei and Marcozzi, Alessio and Mangel, Walter F. and Herrmann, Andreas and van Oijen, Antoine M.},
abstractNote = {In numerous biological processes associations involve a protein with its binding partner, an event that is preceded by a diffusion-mediated search bringing the two partners together. Often hindered by crowding in biologically relevant environments, three-dimensional diffusion can be slow and result in long bimolecular association times. Moreover, the initial association step between two binding partners often represents a rate-limiting step in biotechnologically relevant reactions. We also demonstrate the practical use of an 11-a.a. DNA-interacting peptide derived from adenovirus to reduce the dimensionality of diffusional search processes and speed up associations between biological macromolecules. We functionalize binding partners with the peptide and demonstrate that the ability of the peptide to one-dimensionally diffuse along DNA results in a 20-fold reduction in reaction time. We also show that modifying PCR primers with the peptide sled enables significant acceleration of standard PCR reactions.},
doi = {10.1039/C5SC03063C},
journal = {Chemical Science},
number = 2,
volume = 7,
place = {United States},
year = {Wed Oct 07 00:00:00 EDT 2015},
month = {Wed Oct 07 00:00:00 EDT 2015}
}
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Works referencing / citing this record:
Catalytic transport of molecular cargo using diffusive binding along a polymer track
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