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Peptide self-association in aqueous trifluoroethanol monitored by pulsed field gradient NMR diffusion measurements.

Abstract：

:Defining the self-association state of a molecule in solution can be an important step in NMR-based structure determination. This is particularly true of peptides, where there can be a relatively small number of long-range interactions and misinterpretation of an intermolecular NOE as an intramolecular contact can have a dramatic influence on the final calculated structure. In this paper, we have investigated the use of translational self-diffusion coefficient measurements to detect self-association in aqueous trifluoroethanol of three peptides which are analogues of the C-terminal region of human neuropeptide Y. Experimentally measured diffusion coefficients were extrapolated to D0, the limiting value as the peptide concentration approaches zero, and then converted to D(20,w), the diffusion coefficient after correction for temperature and the viscosity of the solvent. A decrease in D(20,w) of about 16% was found for all three peptides in aqueous TFE (30% by volume) compared with water, which is in reasonable agreement with the expected decrease upon dimerisation, the presence of which was indicated by sedimentation equilibrium measurements. Apparent molecular masses of these peptides in both solutions were also calculated from their diffusion coefficients and similar results were obtained. Several potential internal standards, including acetone, acetonitrile, dimethylsulfoxide and dioxane, were assessed as monitors of solution viscosity over a range of trifluoroethanol concentrations. Compared with independent measurements of viscosity, acetonitrile was the most accurate standard among these four. The practical limitations of a quantitative assessment of peptide self-association from translational diffusion coefficients measured by PFGNMR, including the calculation of apparent molecular mass, are also discussed.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Yao S,Howlett GJ,Norton RS

doi

10.1023/a:1008382624724

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

109-19

issue

2

eissn

0925-2738

issn

1573-5001

journal_volume

16

pub_type

杂志文章

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