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  • Title: Measurement of SDS Micelle-Peptide Association Using (1)H NMR Chemical Shift Analysis and Pulsed-Field Gradient NMR Spectroscopy.
    Author: Orfi L, Lin M, Larive CK.
    Journal: Anal Chem; 1998 Apr 01; 70(7):1339-45. PubMed ID: 21644730.
    Abstract:
    The binding of two simple tripeptides, glycyl-histidyl-glycine (GHG) and phenylalanyl-histidyl-phenylalanine (FHF) with SDS micelles was examined using (1)H NMR chemical shift analysis and self-diffusion coefficients measured with pulsed-field gradient NMR spectroscopy. The presence of GHG or FHF did not appear to significantly affect the critical micelle concentration (cmc) or the average size of the SDS micelles formed. The chemical shifts of several of the GHG resonances change as a function of SDS concentration, indicating an interaction between the peptide and the micelles. In addition, the concentration-dependent decrease observed for the GHG diffusion coefficients suggests association of the peptide with SDS micelles. The free and micelle-associated GHG are in fast exchange on both the (1)H chemical shift and diffusion time scales. The equilibrium constant for the binding of GHG to SDS micelles was determined from the analysis of the concentration dependence of the histidine C2 and C4 resonances to be 17 ± 5 and 24 ± 6 M(-)(1), respectively. The precision of the equilibrium constants obtained by analysis of the chemical shift data is limited by the small chemical shift changes observed. Analysis of the concentration dependence of the diffusion coefficients produced an equilibrium constant of 17 ± 1 M(-)(1). The more hydrophobic peptide, FHF is strongly associated with the SDS micelles. Because the fraction of free FHF is small in these solutions, it was not possible to determine a formation constant for the interaction of FHF with the SDS micelles by analysis of either the (1)H chemical shift or diffusion coefficient data. The cmc of SDS in 0.10 M Na(2)C(2)O(4) buffer was determined to be 5.4 ± 0.1 mM by analysis of the SDS diffusion coefficients in the absence of the peptides. The SDS cmc could also be extracted from the GHG and FHF diffusion coefficients measured as a function of the SDS concentration. The cmc determined from the GHG diffusion data, 5.7 ± 0.2 mM, is in good agreement with the value determined from analysis of the SDS diffusion coefficients in the 5.0 mM GHG solution, 5.2 ± 0.1 mM. The smaller cmc determined from the FHF diffusion data, 4.1 ± 0.1 mM, may reflect some association of the SDS with the peptide prior to micelle formation in bulk solution.
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