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pubmed-article:9706386pubmed:abstractTextThe gradual hydration of phospholipid films can be effectively probed by Fourier transform infrared (FTIR) spectroscopy (cf. part I of this series). The hydration-induced changes observed for lipid IR-absorption bands are probably composed of contributions arising from the effects of both the direct binding of water molecules and the thereby caused conformational changes and phase transitions in the lipid molecules and assemblies, respectively. In this article, an attempt is made to attribute some of the more indicative spectroscopic results to these molecular and supermolecular processes with a view to separating their individual contributions to the relevant spectroscopic data. This is done by considering a series of suitable PLs consisting of the palmitoyl and oleoyl lecithins, DPPC, DOPC, POPC, and OPPC, and one cephalin, DOPE. This choice of PCs and DOPE means that at room temperature and different degrees of hydration, several phase states including lamellar gel and liquid crystalline as well as certain nonlamellar phases are covered. The separation of the water-binding and phase-transition contributions to the FTIR-spectroscopic data, we believe, is clearly demonstrated by interpreting the hydration-dependent wavenumber shifts of the nu C=O band of the PCs. Carbonyl groups are affected to a more significant degree for lipids arrayed in the L alpha phase than in the gel phase. A number of spectral features reveal the lyotropically triggered chain-melting transition as well as other structural rearrangements of PCs. This is discussed in detail and demonstrates the excellent sensitivity of the FTIR methodology for the study of such systems.lld:pubmed
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pubmed-article:9706386pubmed:pagination281-94lld:pubmed
pubmed-article:9706386pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9706386pubmed:year1998lld:pubmed
pubmed-article:9706386pubmed:articleTitleFourier transform infrared spectroscopy as a probe for the study of the hydration of lipid self-assemblies. II. Water binding versus phase transitions.lld:pubmed
pubmed-article:9706386pubmed:affiliationFriedrich-Schiller University Jena, Department of Biophysical Chemistry, Germany.lld:pubmed
pubmed-article:9706386pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9706386pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:9706386pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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