Effect of secondary structure on the interactions of peptide T4 LYS (11-36) in mixtures of aqueous sodium chloride and 2,2,2,-Trifluoroethanol

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Description

The potential of mean force for protein-protein interactions is key to the development of a statistical-mechanical model for salt-induced protein precipitation and crystallization, and for understanding certain disease states, including cataract formation and {beta}-amyloid pathology in Alzheimer's disease. Fluorescence anisotropy provides a method for quantitative characterization of intermolecular interactions due to reversible association. Monomer-dimer equilibria for the peptide T4 LYS(11-36) were studied by fluorescence anisotropy. This peptide, derived from the {beta}-sheet region of the T4 lysozyme molecule, has the potential to form amyloid fibrils. 2,2,2-trifluoroethanol (TFE) induces a change in peptide secondary structure, and was used in aqueous solutions at ... continued below

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34 pages

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Anderson, Camille O.; Spiegelberg, Susanne; Prausnitz, John M. & Blanch, Harvey W. October 1, 2001.

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Description

The potential of mean force for protein-protein interactions is key to the development of a statistical-mechanical model for salt-induced protein precipitation and crystallization, and for understanding certain disease states, including cataract formation and {beta}-amyloid pathology in Alzheimer's disease. Fluorescence anisotropy provides a method for quantitative characterization of intermolecular interactions due to reversible association. Monomer-dimer equilibria for the peptide T4 LYS(11-36) were studied by fluorescence anisotropy. This peptide, derived from the {beta}-sheet region of the T4 lysozyme molecule, has the potential to form amyloid fibrils. 2,2,2-trifluoroethanol (TFE) induces a change in peptide secondary structure, and was used in aqueous solutions at concentrations from 0 to 50% (v/v) at 25 and 37 C to examine the role of peptide conformation on peptide-peptide interactions. The association constant for dimerization increased with rising TFE concentration and with falling temperature. The peptide-peptide potential of mean force was computed from these association constants. Circular-dichroism measurements showed that the secondary structure of the peptide plays an important role in these strong attractive interactions due to intermolecular hydrogen-bond formation and hydrophobic interactions.

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34 pages

Notes

OSTI as DE00837230

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  • Other Information: PBD: 1 Oct 2001

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  • Report No.: LBNL-49227
  • Grant Number: AC03-76SF00098
  • DOI: 10.2172/837230 | External Link
  • Office of Scientific & Technical Information Report Number: 837230
  • Grant Number: CTS 9530793
  • Archival Resource Key: ark:/67531/metadc781618

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  • October 1, 2001

Added to The UNT Digital Library

  • Dec. 3, 2015, 9:30 a.m.

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  • July 26, 2016, 3:31 p.m.

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Anderson, Camille O.; Spiegelberg, Susanne; Prausnitz, John M. & Blanch, Harvey W. Effect of secondary structure on the interactions of peptide T4 LYS (11-36) in mixtures of aqueous sodium chloride and 2,2,2,-Trifluoroethanol, report, October 1, 2001; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc781618/: accessed August 18, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.