help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nuzzo, S.
Right arrow Articles by Morante, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nuzzo, S.
Right arrow Articles by Morante, S.

Biophys J, December 2002, p. 3507-3512, Vol. 83, No. 6

An X-Ray Absorption Spectroscopy Study of the Zinc Environment in Langmuir-Blodgett Phospholipid Multilayers

S. Nuzzo,* C. Meneghini,dagger Dagger S. Mobilioo,Dagger § H. Haas, P. Riccio,|| A. Fasano,** P. Cavatorta,dagger dagger Dagger Dagger and S. MoranteDagger Dagger §§

 *Dipartimento di Fisica, University of Napoli, Italy;  dagger INFM General Purpose Italian Beam Line for Diffraction and Absorption c/o European Synchrotron Radiation Facility Grenoble, France;  Dagger Dipartimento di Fisica Universita' Roma Tre, Italy;  §Laboratori Nazionali di Frascati dell' INFN, Frascati, Italy;  MBT Munich Biotechnology GmbH, Martinsried, Germany;  ||Dipartimento di Biologia, D.B.A.F., University of Basilicata, Potenza, Italy;  **Dipartimento di Biochimica e Biologia Molecolare, University of Bari, Italy;  dagger dagger Dipartimento di Fisica, University of Parma, Italy;  Dagger Dagger Istituto Nazionale per la Fisica della Materia, Italy; and  §§Dipartimento di Fisica, University of Roma Tor Vergata Roma, Italy

For the first time x-ray absorption spectroscopy was used to investigate the Zn environment in Langmuir-Blodgett multilayers. The multilayers were taken as a model of the multilamellar structure of the myelin sheath, the membrane surrounding the nerve axon, which plays a crucial role for signal transduction along the axon. The layers were assembled from the phospholipid dilauroylphosphatidic acid, both in the presence and in the absence of myelin basic protein. The analysis of the extended x-ray absorption fine structure and of the near edge regions of the x-ray absorption spectra at the Zn K-edge provided an accurate description of the local structure showing that the Zn ions are bound to the heads of the phospholipid molecules. The myelin basic protein induces a distortion on the Zn local environment due to a steric constraint but does not substitute the phosphate headgroups. These findings represent an important step in understanding the interplay among myelin basic protein, Zn, and the lipids of the myelin sheath.

Biophys J, December 2002, p. 3507-3512, Vol. 83, No. 6
© 2002 by the Biophysical Society   0006-3495/02/12/3507/06  $2.00




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Biophysical Society.