Fourier transform infrared-attenuated total reflection spectroscopy of hydration of dimyristoylphosphatidylcholine multibilayers

Ter‐Minassian‐Saraga, Lisbeth; Okamura, Emiko; Umemura, Junzo; Takenaka, Tohru

doi:10.1016/0005-2736(88)90417-8

Cited by 83 publications

(46 citation statements)

References 26 publications

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“…Introducing orientation disorder of the hPLB membrane lowers the calculated tilt angle. As a check on the accuracy of the original calculation, the orientation of the ester carbonyl bond of DMPC was found to be 61 ± 10, compared to literature values of 64-65°for well-ordered multilamellar films of DMPC (Nabedryk et al, 1982;Ter-Minassian-Saraga et al, 1988). Compared to transmission dichroism measurements, polarized ATR led to a lower estimate of the a-helix tilt angle of 37 ± 30 (i.e., a-helices are more perpendicular to the membrane plane), with a corresponding order parameter S of 0.44 ± 0.16.…”

Section: Resultsmentioning

confidence: 89%

Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban

Ludlam

Arkin

Liu

et al. 1996

Biophysical Journal

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Phospholamban is a 52-amino acid residue membrane protein that regulates Ca(2+)-ATPase activity in the sarcoplasmic reticulum of cardiac muscle cells. The hydrophobic C-terminal 28 amino acid fragment of phospholamban (hPLB) anchors the protein in the membrane and may form part of a Ca(2+)-selective ion channel. We have used polarized attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy along with site-directed isotope labeling to probe the local structure of hPLB. The frequency and dichroism of the amide I and II bands appearing at 1658 cm-1 and 1544 cm-1, respectively, show that dehydrated and hydrated hPLB reconstituted into dimyristoylphosphatidycholine bilayer membranes is predominantly alpha-helical and has a net transmembrane orientation. Specific local secondary structure of hPLB was probed by incorporating 13C at two positions in the protein backbone. A small band seen near 1614 cm-1 is assigned to the amide I mode of the 13C-labeled amide carbonyl group(s). The frequency and dichroism of this band indicate that residues 39 and 46 are alpha-helical, with an axial orientation that is approximately 30 degrees relative to the membrane normal. Upon exposure to 2H2O (D2O), 30% of the peptide amide groups in hPLB undergo a slow deuterium/hydrogen exchange. The remainder of the protein, including the peptide groups of Leu-39 and Leu-42, appear inaccessible to exchange, indicating that most of the hPLB fragment is embedded in the lipid bilayer. By extending spectroscopic characterization of PLB to include hydrated, deuterated as well as site-directed isotope-labeled hPLB films, our results strongly support models of PLB that predict the existence of an alpha-helical hydrophobic region spanning the membrane domain.

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Section: Resultsmentioning

confidence: 89%

Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban

Ludlam

Arkin

Liu

et al. 1996

Biophysical Journal

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“…Between 1705 and 1680 cm −1 , appears a band associated to β-sheet anti-parallel, occurring normally at 1701 cm −1 , and β-turn, observed for others [29] at 1685 cm −1 . The band at 1460 cm −1 may be assigned to C-OH in-plane bend due to oligosaccharide chains [30] of the GPI anchor, but could be also attributed to C-H scissoring in CH 2 and CH 3 [31], present at the hydrophobic moiety of the GPI anchor.…”

Section: Pure Oap At the Air-water Interface: Surface Pressureand Potmentioning

confidence: 99%

Rat osseous plate alkaline phosphatase as Langmuir monolayer—An infrared study at the air–water interface

Caseli

Masui

Furriel

et al. 2008

Journal of Colloid and Interface Science

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“…phosphate and carbonyl, and not to other water molecules. IR spectroscopy has been extensively used to characterize the hydration sites of PC showing that the primary hydration site is the phosphate group (Arrondo et al 1984;Ter-Minassian-Saraga et al 1988;Grdadolnik et al 1991). Thus, the observed shift of the OH stretching band to lower frequencies is in accordance with the expected stronger hydrogen bonds between water molecules and phosphate groups relative to water-water hydrogen bonds (Bhide and Berkowitz 2005).…”

Section: Dehydration Of Multibilayers By Water Evaporation and Osmotimentioning

confidence: 78%

Long-Range Lipid-Water Interaction as Observed by ATR-FTIR Spectroscopy

Arsov

2015

Subcellular Biochemistry

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It is commonly assumed that the structure of water at a lipid-water interface is influenced mostly in the first hydration layer. However, recent results from different experimental methods show that perturbation extends through several hydration layers. Due to its low light penetration depth, attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy is specifically suited to study interlamellar water structure in multibilayers. Results obtained by this technique confirm the long-range water structure disturbance. Consequently, in confined membrane environments nearly all water molecules can be perturbed. It is important to note that the behavior of confined water molecules differs significantly in samples prepared in excess water and in partially hydrated samples. We show in what manner the interlamellar water perturbation is influenced by the hydration level and how it is sequentially modified with a step-by-step dehydration of samples either by water evaporation or by osmotic pressure. Our results also indicate that besides different levels of hydration the lipid-water interaction is modulated by different lipid headgroups and different lipid phases as well. Therefore, modification of interlamellar water properties may clarify the role of water-mediated effects in biological processes.

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Fourier transform infrared-attenuated total reflection spectroscopy of hydration of dimyristoylphosphatidylcholine multibilayers

Cited by 83 publications

References 26 publications

Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban

Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban

Rat osseous plate alkaline phosphatase as Langmuir monolayer—An infrared study at the air–water interface

Long-Range Lipid-Water Interaction as Observed by ATR-FTIR Spectroscopy

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