We have performed a quantitative analysis of the X-ray absorption near-edge structure (XANES) spectra at the Zinc K-edge of systems formed by phospholipid Langmuir-Blodgett multilayers (LBMLs) in the presence and in the absence of myelin basic protein (MBP) and in two hydration conditions. These spectra have been analysed by a new procedure called Minuit XANes (MXAN) which is able to perform a quantitative fit of XANES data in terms of structural parameters. By this method, we have been able to correlate the relevant differences between the spectra observed in the XANES range with the coordination changes due to reduction of the space around the Zinc when the level of hydration is lowered and/or the myelin basic protein is added. These spectral differences are peculiar of the XANES energy range, and are not present in the extended X-ray absorption fine structure (EXAFS) energy range where the analysis was previously performed. With this investigation, we give an unambiguous answer to the question of the role of zinc in such complexes by showing that the metal interacts with both the phospholipid heads of the substrate and the myelin basic protein. (C) 2004 Elsevier B.V All rights reserved.
Benfatto, M., Della Longa, S., Qin, Y., Li, Q., Pan, G., Wu, Z., et al. (2004). The role of Zn in the interplay among Langmuir-Blodgett multilayer and myelin basic protein: a quantitative analysis of XANES spectra. BIOPHYSICAL CHEMISTRY, 110, 191-201 [10.1016/j.bpc.2004.02.003].
The role of Zn in the interplay among Langmuir-Blodgett multilayer and myelin basic protein: a quantitative analysis of XANES spectra
MORANTE, SILVIA
2004-01-01
Abstract
We have performed a quantitative analysis of the X-ray absorption near-edge structure (XANES) spectra at the Zinc K-edge of systems formed by phospholipid Langmuir-Blodgett multilayers (LBMLs) in the presence and in the absence of myelin basic protein (MBP) and in two hydration conditions. These spectra have been analysed by a new procedure called Minuit XANes (MXAN) which is able to perform a quantitative fit of XANES data in terms of structural parameters. By this method, we have been able to correlate the relevant differences between the spectra observed in the XANES range with the coordination changes due to reduction of the space around the Zinc when the level of hydration is lowered and/or the myelin basic protein is added. These spectral differences are peculiar of the XANES energy range, and are not present in the extended X-ray absorption fine structure (EXAFS) energy range where the analysis was previously performed. With this investigation, we give an unambiguous answer to the question of the role of zinc in such complexes by showing that the metal interacts with both the phospholipid heads of the substrate and the myelin basic protein. (C) 2004 Elsevier B.V All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
