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Weak interactions between folate and osmolytes in solution.

Michael R Duff1, Jordan Grubbs, Engin Serpersu

  • 1Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840, United States.

Biochemistry
|February 29, 2012
PubMed
Summary
This summary is machine-generated.

Osmolytes like betaine and DMSO weaken folate binding to enzymes by interacting directly with folate. This competition explains reduced enzyme activity under osmotic stress in cellular environments.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Osmotic stress affects enzyme-substrate binding, particularly dihydrofolate reductase (DHFR) with dihydrofolate (DHF).
  • Previous studies indicated weaker DHF binding to DHFRs in the presence of osmolytes, suggesting competition for DHF.
  • This competition hypothesis requires direct interactions between osmolytes and DHF or its analogs.

Purpose of the Study:

  • To evaluate the hypothesis that osmolytes compete with DHFR for DHF binding.
  • To investigate the direct interactions between osmolytes and folate or its fragments.
  • To understand the role of these weak interactions in the cellular environment.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to monitor folate dimerization and osmolyte interactions.
  • Nuclear Overhauser Effect (NOE) spectroscopy to assess changes in molecular tumbling rates.
  • Osmotic stress experiments to determine osmolyte-ligand interactions.

Main Results:

  • Betaine and DMSO weakened folate dimerization, indicating preferential interaction with folate monomers.
  • NOE experiments showed decreased tumbling rates upon osmolyte addition, consistent with direct interactions.
  • Osmotic stress experiments confirmed preferential interactions of betaine, DMSO, and sucrose with folate and its fragments.

Conclusions:

  • Os сайтыmolytes preferentially interact with folate, competing with enzyme binding.
  • These weak interactions are significant in crowded cellular environments, impacting specific binding events.
  • Understanding osmolyte-folate interactions provides insights into enzyme regulation under physiological stress.