FTIR spectroscopy in biomedical research: how to get the most out of its potential

Magalhães, Sandra; Goodfellow, Brian J.; Nunes, Alexandra

doi:10.1080/05704928.2021.1946822

Cited by 38 publications

(16 citation statements)

References 199 publications

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“…Now, we intended to verify if spectroscopic approaches can be used for protein aggregation studies in aging biofluids, using a new independent dataset of plasma samples to validate our previous results. Despite the experimental procedures being the same in our previous work (9) and here, we adjusted our spectral processing method to more accurately analyze the spectra, according to what is reported in the literature (10): specifically, we normalized spectra to the total area of the amide I band and not to the intensity of the amide I peak. Nevertheless, our results coincide with those from our first cohort of samples and show that from middle to old age, there seems to be a transition from prefibrillar to fibrillar structures in proteins in blood plasma.…”

Section: Discussionmentioning

confidence: 99%

“…Similar to our previous work, spectra were visually analyzed individually to detect suspicious profiles or high background noise. An exploratory PCA analysis was also performed on raw spectra to detect outlier samples based on Q-residuals and Hotelling's T 2 values (10). After outlier removal, the region of interest (1700-1600cm -1 ) was selected, baseline corrected and area normalized, to correct for differences in que amount of sample placed on the crystal.…”

Section: Ftir Measurements and Data Analysismentioning

confidence: 99%

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FTIR spectroscopy confirms age-related changes in protein conformation in a new independent dataset of human plasma samples

Magalhães

Teixeira²,

Gouveia³

et al. 2022

MARJ

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The loss of proteostasis is a key hallmark of aging and has been well documented using several model systems. However, in biofluids such as blood plasma, little is known about how the loss of proteostasis affects protein conformation during aging. Our previous work has demonstrated age-related changes in protein conformation in human plasma samples using FTIR spectroscopy and conformation-specific antibodies. To prove the potential of spectroscopy to detect slight changes in protein secondary structure during aging, we have applied the same methodology to a new and independent set of 24 human plasma samples from donors with ages ranging from 40 to 75 years. The results clearly show that from middle to old age there is a decrease in antiparallel β-sheet structures and an increase in intermolecular β-sheets, indicative of an increase in aggregation-prone proteins in human plasma over time. This confirms the potential of FTIR spectroscopy as a technique to evaluate protein conformational changes related to health and disease and as a suitable method to be used in a clinical setting to produce quick and reliable results.

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Section: Discussionmentioning

confidence: 99%

Section: Ftir Measurements and Data Analysismentioning

confidence: 99%

FTIR spectroscopy confirms age-related changes in protein conformation in a new independent dataset of human plasma samples

Magalhães

Teixeira²,

Gouveia³

et al. 2022

MARJ

Self Cite

View full text Add to dashboard Cite

show abstract

“…All spectra were individually visually analyzed and spectra with background noise or with suspicious profile were repeated to ensure good quality data. After visual inspection, a PCA analysis was performed to identify and remove outliers, as previously described (reviewed in [ 60 ]). Samples with high values for PCA Q-residuals were considered outliers and removed from data matrix.…”

Section: Methodsmentioning

confidence: 99%

The Long-Term Culture of Human Fibroblasts Reveals a Spectroscopic Signature of Senescence

Magalhães

Almeida

Pereira

et al. 2022

IJMS

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Aging is a complex process which leads to progressive loss of fitness/capability/ability, increasing susceptibility to disease and, ultimately, death. Regardless of the organism, there are some features common to aging, namely, the loss of proteostasis and cell senescence. Mammalian cell lines have been used as models to study the aging process, in particular, cell senescence. Thus, the aim of this study was to characterize the senescence-associated metabolic profile of a long-term culture of human fibroblasts using Fourier Transform Infrared and Nuclear Magnetic Resonance spectroscopy. We sub-cultivated fibroblasts from a newborn donor from passage 4 to passage 17 and the results showed deep changes in the spectroscopic profile of cells over time. Late passage cells were characterized by a decrease in the length of fatty acid chains, triglycerides and cholesterol and an increase in lipid unsaturation. We also found an increase in the content of intermolecular β-sheets, possibly indicating an increase in protein aggregation levels in cells of later passages. Metabolic profiling by NMR showed increased levels of extracellular lactate, phosphocholine and glycine in cells at later passages. This study suggests that spectroscopy approaches can be successfully used to study changes concomitant with cell senescence and validate the use of human fibroblasts as a model to monitor the aging process.

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“…It is unquestionable that the quality and relevance of the information collected through spectral analysis and the potential application of the information collected in clinical practice, such as diagnosis and prognosis, is only possible using multivariate analysis tools. Additional information about these tools and their application in data analysis can be found in [94][95][96].…”

Section: Sample Type Acquisition Conditions Analysis Type Main Findin...mentioning

confidence: 99%

Metabolic Profile Characterization of Different Thyroid Nodules Using FTIR Spectroscopy: A Review

et al. 2022

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Thyroid cancer’s incidence has increased in the last decades, and its diagnosis can be a challenge. Further and complementary testing based in biochemical alterations may be important to correctly identify thyroid cancer and prevent unnecessary surgery. Fourier-transform infrared (FTIR) spectroscopy is a metabolomic technique that has already shown promising results in cancer metabolome analysis of neoplastic thyroid tissue, in the identification and classification of prostate tumor tissues and of breast carcinoma, among others. This work aims to gather and discuss published information on the ability of FTIR spectroscopy to be used in metabolomic studies of the thyroid, including discriminating between benign and malignant thyroid samples and grading and classifying different types of thyroid tumors.

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FTIR spectroscopy in biomedical research: how to get the most out of its potential

Cited by 38 publications

References 199 publications

FTIR spectroscopy confirms age-related changes in protein conformation in a new independent dataset of human plasma samples

FTIR spectroscopy confirms age-related changes in protein conformation in a new independent dataset of human plasma samples

The Long-Term Culture of Human Fibroblasts Reveals a Spectroscopic Signature of Senescence

Metabolic Profile Characterization of Different Thyroid Nodules Using FTIR Spectroscopy: A Review

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