Conformational features of lipids and proteins in myelin membranes using Raman and infrared spectroscopy

Carmona, Pedro; Ramos, J.M.; Cozar, M. de; Monreal, J.

doi:10.1002/jrs.1250180704

Cited by 11 publications

(9 citation statements)

References 31 publications

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“…A variety of structural and biophysical techniques, including spectroscopy, electron spin resonance, deuteron NMR, freeze-fracture electron microscopy, and X-ray diffraction, have been applied to systems consisting of various single lipid components (e.g., lecithin, dimyristoyllecithin) reconstituted with either proteolipid protein and its associated lipids or with the proteolipid protein devoid of associated lipids (the proteolipid apoprotein). Previous research has focused on the interactions between PLP and the lipid component, the structure of PLP and its effect on lipid organization in the bilayer, and the ionophoric properties of PLP (Curatolo et al, 1977;Brady et al, 1979;Rice et al, 1979;Ting-Beall et al, 1979;Lin and Lees, 1982;Helynck et al, 1983;Brophy et al, 1984;Brown et al, 1985; Garcia-Segura et a]., 1985; Carmona et al, 1987;DeCozar et al, 1987;Meier et al, 1987;Surewicz et al, 1987). What has not been addressed in these and related studies is whether the reconstitution of PLP with lipids allows the protein to form stable inter-bilayer contacts like those inferred from studies on undisrupted myelin.…”

Section: Introductionmentioning

confidence: 99%

X‐ray diffraction analysis of myelin lipid/proteolipid protein multilayers

Brown¹,

Karthigasan²,

Singh³

et al. 1989

J of Neuroscience Research

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To examine the proposal that myelin proteolipid protein underlies the adhesion of neighboring membranes in central nervous system (CNS) myelin, we carried out X-ray diffraction studies on the structure and interactions of model bilayers composed of total myelin lipids plus proteolipid apoprotein (PLP). Total myelin lipids were used because their heterogeneity was expected to provide an appropriate environment for the integral membrane protein to achieve its native conformation and establish appropriate contacts with the apposed bilayer. We found that incorporation of PLP into myelin lipid bilayers, whether organized into multilamellar vesicles or oriented multilayers, did not appreciably affect the lamellar period, which ranged from 65-71 A. In oriented multilayers, the wide-angle spacing at approximately 4.8 A, which arises from the lateral packing of lipid chains and is perpendicular to the lamellar diffraction, was less oriented and weaker in bilayers containing the protein. These results indicate that PLP was incorporated into the bilayers and had a disordering effect on the hydrocarbon chains but did not extend into the spaces between bilayers. Bilayer profiles calculated from the lamellar diffraction to about 15 A spacing did not show any major changes in the distribution of electron density, suggesting that to moderate resolution, the protein was distributed uniformly across the width of the lipid bilayer. Periodicities measured from osmotically stressed multilamellar vesicles did not depend on the presence of PLP, indicating that the protein did not form stabilizing contacts between bilayers.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Introductionmentioning

confidence: 99%

X‐ray diffraction analysis of myelin lipid/proteolipid protein multilayers

Brown¹,

Karthigasan²,

Singh³

et al. 1989

J of Neuroscience Research

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“…The symmetric and asymmetric vibrational modes of the CH 2 and CH3 groups can offer information about interactions between hydrocarbon chains. The peak height intensity relations Iν s CH 2 /Iν as CH 2 (I2850/I2890) and Iν s CH 3 /Iν as CH 3 (I2935/I2890) offer valuable indices to measure lipid packing consequences and establish relative order/disorder of the intermolecular lipid chain [ 36 , 37 ].…”

Section: Basic Concepts Of Vibrational Spectroscopic Techniques: Imentioning

confidence: 99%

Development of Meat Products with Healthier Lipid Content: Vibrational Spectroscopy

Ruíz‐Capillas

Herrero

2021

Foods

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This review focuses on the importance of developing meat products with healthier lipid content and strategies such as the use of structured lipids to develop these enriched products. The review also conducts a critical analysis of the use of vibrational spectroscopy as a tool to further these developments. Meat and meat products are extensively recognized and consumed in the world. They are an important nutritional contribution in our diet. However, their consumption has also been associated with some negative consequences for health due to some of its components. There are new trends in the design of healthy meat products focusing mainly on improving their composition. From among the different strategies, improving lipid content is the one that has received the most attention. A novel development is the formation of lipid materials based on structured lipids such emulsion gels (EGs) or oil-bulking agents (OBAs) that offer attractive applications in the reformulation of health-enhanced meat products. A deeper interpretation is required of the complicated relationship between the structure of their components and their properties in order to obtain structured lipids and healthier meat products with improved lipid content and acceptable characteristics. To this end, vibrational spectroscopy techniques (Raman and infrared spectroscopy) have been demonstrated to be suitable in the elucidation of the structural characteristics of lipid materials based on structured lipids (EGs or OBAs) and the corresponding reformulated health-enhanced meat products into which these fat replacers have been incorporated. Future research on these structures and how they correlate to certain technological properties could help in selecting the best lipid material to achieve specific technological properties in healthier meat products with improved lipid content.

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“…The 1630 cm -1 peak is more difficult to interpret from the viewpoint of protein configuration, however, according to Pedro's [49] and Zanyar's work [50], it could be ascertained that 1630cm -1 is corresponded to protein amide I β-structure from myelin membranes. As shown in Fig.…”

Section: Relative Spectral Contributions In Health 14 Dpi and 14 Dltmentioning

confidence: 99%

Label-Free Spectral Imaging Unveils Biochemical Mechanisms of Low-Level Laser Therapy on Spinal Cord Injury

Gong

Wang

Liang

et al. 2018

Cell Physiol Biochem

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Background/Aims: Low-level laser therapy (LLLT) leads to complex photochemical responses during the healing process of spinal cord injury (SCI). Confocal Raman Microspectral Imaging (in combination with multivariate analysis) was adopted to illustrate the underlying biochemical mechanisms of LLLT treatment on a SCI rat model. Methods: Using transversal tissue sections, the Raman spectra can identify areas neighboring the injury site, glial scar, cavity, and unharmed white matter, as well as their correlated cellular alterations, such as demyelination and up-regulation of chondroitin sulfate proteoglycans (CSPGs). Multivariate data analysis methods are used to depict the underlying therapeutic effects by highlighting the detailed content and distribution variations of the biochemical constituents. Results: It is confirmed that photon-tissue interactions might lead to a decay of the inhibitory response to remyelination by suppressing CSPG expression, as also morphologically demonstrated by reduced glial scar and cavity areas. An inter-group comparison semi-quantitatively confirms changes in lipids, phosphatidic acid, CSPGs, and cholesterol during SCI and its LLLT treatment, paving the way for in vitro and in vivo understanding of the biochemical changes accompanying pathobiological SCI events. Conclusion: The achieved results in this work not only have once again proved the well-known cellular mechanisms of SCI, but further illustrate the underlying biochemical variability during LLLT treatment, which provide a sound basis for developing real-time Raman methodologies to monitor the efficacy of the SCI LLLT treatment.

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Conformational features of lipids and proteins in myelin membranes using Raman and infrared spectroscopy

Cited by 11 publications

References 31 publications

X‐ray diffraction analysis of myelin lipid/proteolipid protein multilayers

X‐ray diffraction analysis of myelin lipid/proteolipid protein multilayers

Development of Meat Products with Healthier Lipid Content: Vibrational Spectroscopy

Label-Free Spectral Imaging Unveils Biochemical Mechanisms of Low-Level Laser Therapy on Spinal Cord Injury

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