FTIR Analysis of Proteins and Protein–Membrane Interactions

Tatulian, Suren A.

doi:10.1007/978-1-4939-9512-7_13

Cited by 53 publications

(37 citation statements)

References 124 publications

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“…This could affect the structural change in PDI that is required for disassembly of the CT holotoxin. We examined this possibility with Fourier transform-infrared (FTIR) spectroscopy, a technique that can detect changes in the secondary and tertiary structures of proteins [44,45]. As seen in Figure 4A, the spectrum of PDI (dashed line) did not shift or change shape in the presence of a 150-fold molar excess of Q3R (grey solid line).…”

Section: Resultsmentioning

confidence: 99%

Quercetin-3-Rutinoside Blocks the Disassembly of Cholera Toxin by Protein Disulfide Isomerase

Guyette

Cherubin

Serrano

et al. 2019

Toxins

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Protein disulfide isomerase (PDI) is mainly located in the endoplasmic reticulum (ER) but is also secreted into the bloodstream where its oxidoreductase activity is involved with thrombus formation. Quercetin-3-rutinoside (Q3R) blocks this activity, but its inhibitory mechanism against PDI is not fully understood. Here, we examined the potential inhibitory effect of Q3R on another process that requires PDI: disassembly of the multimeric cholera toxin (CT). In the ER, PDI physically displaces the reduced CTA1 subunit from its non-covalent assembly in the CT holotoxin. This is followed by CTA1 dislocation from the ER to the cytosol where the toxin interacts with its G protein target for a cytopathic effect. Q3R blocked the conformational change in PDI that accompanies its binding to CTA1, which, in turn, prevented PDI from displacing CTA1 from its holotoxin and generated a toxin-resistant phenotype. Other steps of the CT intoxication process were not affected by Q3R, including PDI binding to CTA1 and CT reduction by PDI. Additional experiments with the B chain of ricin toxin found that Q3R could also disrupt PDI function through the loss of substrate binding. Q3R can thus inhibit PDI function through distinct mechanisms in a substrate-dependent manner.

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Section: Resultsmentioning

confidence: 99%

Quercetin-3-Rutinoside Blocks the Disassembly of Cholera Toxin by Protein Disulfide Isomerase

Guyette

Cherubin

Serrano

et al. 2019

Toxins

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“…However, these claims are disputed by Goormaghtigh et al, who suggest that Amide III bands are irrelevant when you have obtained information from the 1545 cm −1 Amide II band [49]. Others imply that the Amide III band is significantly affected by side chains, and will be altered by the amino acid composition [62]. Therefore, the majority of research still uses Amide I and II bands for effective analysis and structure elucidation.…”

Section: Atr-ftir Spectroscopy To Characterise Biopharmaceuticalsmentioning

confidence: 99%

ATR-FTIR spectroscopy and spectroscopic imaging for the analysis of biopharmaceuticals

Tiernan

Byrne

Kazarian

2020

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

151

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Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) spectroscopy is a label-free, non-destructive technique that can be applied to a vast range of biological applications, from imaging cancer tissues and live cells, to determining protein content and protein secondary structure composition. This review summarises the recent advances in applications of ATR-FTIR spectroscopy to biopharmaceuticals, the application of this technique to biosimilars, and the current uses of FTIR spectroscopy in biopharmaceutical production. We discuss the use of ATR-FTIR spectroscopic imaging to investigate biopharmaceuticals, and finally, give an outlook on the possible future developments and applications of ATR-FTIR spectroscopy and spectroscopic imaging to this field. Throughout the review comparisons will be made between FTIR spectroscopy and alternative analytical techniques, and areas will be identified where FTIR spectroscopy could perhaps offer a better alternative in future studies. This review focuses on the most recent advances in the field of using ATR-FTIR spectroscopy and spectroscopic imaging to characterise and evaluate biopharmaceuticals, both in industrial and academic research based environments.

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“…IR spectroscopy is widely used for studying the biological objects, especially for the conformational analysis of proteins [3,4,5,6,7,8]. So far, it is widely accepted that the protein-peptide group has nine characteristic absorption bands: amide A (~3300 cm −1 ), amide B (~3100 cm −1 ), amide I (~1650 cm −1 ), amide II (~1550 cm −1 ), amide III (~1300 cm −1 ), amide IV (~735 cm −1 ), amide V (~635 cm −1 ), amide VI (~600 cm −1 ), and amide VII (~200 cm −1 ) [8,9].…”

Section: Introductionmentioning

confidence: 99%

Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

et al. 2019

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Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

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FTIR Analysis of Proteins and Protein–Membrane Interactions

Cited by 53 publications

References 124 publications

Quercetin-3-Rutinoside Blocks the Disassembly of Cholera Toxin by Protein Disulfide Isomerase

Quercetin-3-Rutinoside Blocks the Disassembly of Cholera Toxin by Protein Disulfide Isomerase

ATR-FTIR spectroscopy and spectroscopic imaging for the analysis of biopharmaceuticals

Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

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