NDLI: Speeding up biomolecular interactions by molecular sledding

Content Provider	Royal Society of Chemistry (RSC)
Author	Turkin, Alexander Herrmann, Andreas Marcozzi, Alessio Mangel, Walter F. Zhang, Lei Oijen, Antoine M. van
Copyright Year	2016
Abstract	Numerous biological processes involve association of 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. Similarly, the initial association step between two binding partners often represents a rate-limiting step in biotechnologically relevant reactions. We 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.
Starting Page	916
Ending Page	920
Page Count	5
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	7
Issue Number	2
Journal	Chemical Science
DOI	10.1039/c5sc03063c
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Polymerase chain reaction Adenoviridae DNA Diffusion Peptide Protein
Content Type	Text
Resource Type	Article
Subject	Chemistry

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Speeding up biomolecular interactions by molecular sledding

Speeding up biomolecular interactions by molecular sledding †

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Speeding up biomolecular interactions by molecular sledding† †Electronic supplementary information (ESI) available: Synthesis procedures, experimental procedures and Fig. S1–S11. See DOI: 10.1039/c5sc03063c Click here for additional data file.

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