Conformational changes, from β-strand to α-helix, of the fatty acid-binding protein ReP1-NCXSQ in anionic lipid membranes: dependence with the vesicle curvature

Galassi, Vanesa Viviana; Salinas, Silvina R.; Montich, Guillermo G.

doi:10.1007/s00249-017-1243-5

Cited by 3 publications

(2 citation statements)

References 54 publications

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“…5 shows the presence of five peaks 1683, 1667, 1652, 1637 and 1621 cm −1 obtained after the results of the curve fitting analysis for control and treated samples. The peak due of 1621 cm −1 , 1637 cm −1 assigns to β sheet; 1652 and 1667 cm −1 assigns to α helix and 1683 cm −1 due to antiparallel β sheet [16,40]. It is observed from Table 4 that the percentage area of α helix declines by 3-7% and an increase in β sheet structure by 13-40% was noticed.…”

Section: Ftir Self Deconvolution Deduced By Curve Fitting Analysis In the Amide I Regionmentioning

confidence: 85%

Spectral profile index changes as biomarker of toxicity in Catla catla (Hamilton, 1822) edible fish studied using FTIR and principle component analysis

Kumar¹,

Kumari²,

Kavitha

et al. 2020

SN Appl. Sci.

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The study was carried out to evaluate the toxicity in gill tissue of edible fish Catla catla using FTIR spectra. Fourier selfdeconvolution obtained by curve fitting was applied in the lipid (3000-2800 cm −1 ), carbohydrates (1000-1100 cm −1 ) and in the amide region (1700-1600 cm −1 ). These spectral changes were used as biochemical parameters to assess the degree of toxicity. A disorder in lipid changes was measured by frequency shift and intensity changes in the CH 2 asymmetric stretching band. This change in the fatty acid composition in fish could be used as biomarkers of toxic effect. Decreases in lactic acid (6-16%) clarify the lipid peroxidation which is the primary mechanism of toxicity. The deconvolution in the amide region shows peaks at 1621 cm −1 , 1637 cm −1 due to β sheet; 1652 cm −1 and 1667 cm −1 due to α helix and 1683 cm −1 due to antiparallel β sheet. The results show a decrease by (3-7%) in α helix and increase by (13-40%) in β sheet structure. This shows β sheet formation of protein secondary structure due to toxicity. PCA plots indicate protein and lipids have strong positive loadings. The study shows the spectral variation is considered as an ideal biomarker with a high degree of accuracy of test organism to examine the toxicity of pollutants.

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Section: Ftir Self Deconvolution Deduced By Curve Fitting Analysis In the Amide I Regionmentioning

confidence: 85%

Spectral profile index changes as biomarker of toxicity in Catla catla (Hamilton, 1822) edible fish studied using FTIR and principle component analysis

Kumar¹,

Kumari²,

Kavitha

et al. 2020

SN Appl. Sci.

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show abstract

“…All spectral data were processed with the OMNIC 8.3.103 Software suite (Thermo Fisher Scientific Inc.) The spectral contribution of the 2 H 2 O solution was eliminated from the FTIR spectra of nisin and nisin/DPPG by subtracting the absorbance of the 2 H 2 O solution acquired at the corresponding temperature; this procedure yields the baseline correction in the region of the Amide I band [38]. Each Raman spectrum was baseline corrected in the entire spectral range, while no solvent subtraction was applied to these spectra because of the negligible spectral contribution of water.…”

Section: Discussionmentioning

confidence: 99%

Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: a vibrational study

Morales

Juárez

Montich

et al. 2019

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Interactions between the antibiotic peptide nisin and multilamellar vesicles of phosphoglycerol lipids in different phase-states were studied using vibrational spectroscopy. The infrared amide I' band of nisin, both in solution and in the membrane-bound state, was analyzed in the temperature range comprised between 20 and 60°C in order to study its conformational behavior. Nisin presented mainly unordered and -turns conformations. Their relative populations varied according to the environment and as the temperature increased: β turns were more favored in the membrane-bound state than in solution, but at higher temperatures the disordered conformation was dominant in both states. Spectral changes of specific infrared bands belonging to the hydrocarbon and polar moieties of lipids were also analyzed to evaluate the perturbation of the lipid membrane order. Nisin interactions with the membrane polar region induced a high restriction to water incorporation, promoting a small increase in the temperature of the lipid phase transition. Raman spectra of nisin/phosphoglycerol systems at ambient temperature were also analyzed. They revealed that the peptide incorporation to a membrane in the fluid phase

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Thermal unfolding of calreticulin. Structural and thermodynamic characterization of the transition

Decca

Borioli

Durand

et al. 2019

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Conformational changes, from β-strand to α-helix, of the fatty acid-binding protein ReP1-NCXSQ in anionic lipid membranes: dependence with the vesicle curvature

Cited by 3 publications

References 54 publications

Spectral profile index changes as biomarker of toxicity in Catla catla (Hamilton, 1822) edible fish studied using FTIR and principle component analysis

Spectral profile index changes as biomarker of toxicity in Catla catla (Hamilton, 1822) edible fish studied using FTIR and principle component analysis

Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: a vibrational study

Thermal unfolding of calreticulin. Structural and thermodynamic characterization of the transition

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