Use of time-resolved fluorescence spectroscopy to evaluate diagnostic value of collagen degradation products

Sikora, Joanna; Cyrankiewicz, Michał; Wybranowski, Tomasz; Ziomkowska, Blanka; Ośmiałowski, Borys; Obońska, Ewa; Augustyńska, Beata; Kruszewski, Stefan; Kubica, Jacek

doi:10.1117/1.jbo.20.5.051039

Cited by 5 publications

(3 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Chromatographic assay simply in combination with fluorescence spectroscopy makes up a further method employed for the evaluation of collagen degradation products …”

Section: Structural Analysis Of Collagenmentioning

confidence: 99%

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Rýglová

Braun

Suchý

2017

Macromol. Mater. Eng.

View full text Add to dashboard Cite

Many connective tissue diseases and defects are associated with poor synthesis or excessive degradation of collagen. The modern tissue engineering approach is to replace the defective site via the implantation of a biocompatible scaffold which serves as a carrier for cell incorporation, proliferation, and growth. Collagen is widely used in the field of clinical medicine in connection with both hard and soft tissue applications. However, certain collagen properties such as poor dimensional stability, poor in vivo mechanical strength, low degree of elasticity, variable nature in terms of enzymatic degradation, crosslinking density, fiber size, trace impurities, and side effects frequently limit both its analysis and application. This review focuses particularly on the processing and modification of collagen type I with respect to its biological and mechanical properties. The processing of collagen into scaffolds is crucial to mimic successfully the extracellular matrices. Moreover, the review suggests several ways in which the most common problems related to the isolation, handling, electrospinning, and crosslinking of collagen can be overcome while maintaining its native character as much as possible. Further, the review provides a summary of the analytical methods available for the physicochemical characterization of collagen with respect to both its molecular and submolecular structure.

show abstract

“…Chromatographic assay simply in combination with fluorescence spectroscopy makes up a further method employed for the evaluation of collagen degradation products …”

Section: Structural Analysis Of Collagenmentioning

confidence: 99%

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Rýglová

Braun

Suchý

2017

Macromol. Mater. Eng.

View full text Add to dashboard Cite

show abstract

“…The real distribution of FLTs in such a system is probably much more complex, especially when one realizes that different conformations of the same specimen may exhibit different deactivations of the excited state that would require a much more extensive (and difficult to implement) model. The results of our previous study revealed that the increase in the concentration of hydrolysed collagen added to plasma reduced the fluorescence lifetime at 450 nm depending on the degree of hydrolysis 28 . Aldehydes react with various amino acids in protein and then form several fluorescent compounds in a process called protein lipoxidation 29 , 30 .…”

Section: Resultsmentioning

confidence: 88%

A study of the oxidative processes in human plasma by time-resolved fluorescence spectroscopy

Wybranowski

Ziomkowska

Cyrankiewicz

et al. 2022

Sci Rep

Self Cite

View full text Add to dashboard Cite

The aim of this study was to examine the usefulness of time-resolved fluorescence spectroscopy in the evaluation of the oxidative processes in human plasma. To investigate the impact of oxidative stress on the fluorescence of plasma, five studied markers (thiobarbituric acid-reactive substances, ischemia modified albumin, carbonyl groups, hydrogen peroxide, advanced oxidation protein products) were chosen as oxidative damage approved markers. Our method presents several advantages over traditional methods as it is a direct, non-time-consuming, repeatable, and non-invasive technique that requires only simple pre-treatment of samples without additional reagents and the sample size needed for analysis is small. In principle, each modification of the protein in plasma can be expected to modify its fluorescence properties and hence its lifetime or intensity. The study involved 59 blood donors with no evidence of disease. The research was conducted at excitation wavelengths of 280 nm and 360 nm, and emission was measured at wavelengths of 350 nm and 440 nm, respectively. Our results, although preliminary, suggest that the application of fluorescence measurements can be considered as an effective marker of oxidative stress. Regression analyses showed that a notable growth in fluorescence intensity at 440 nm and a simultaneous decrease in fluorescence intensity and mean fluorescence lifetime at 350 nm are associated with higher levels of oxidative stress.

show abstract

“…Meanwhile, an increase in the concentration of collagen degradation products in blood circulation during the process of lung remodeling in the early phase of wound healing may determine the extent of pulmonary fibrosis. The results of our previous study revealed that an increase in the concentration of hydrolysed collagen added to plasma reduced the mean fluorescence lifetime at 450 nm [ 27 ]. Moreover, the decrease in mean fluorescence lifetime was dependent on the degree of collagen hydrolysis.…”

Section: Introductionmentioning

confidence: 99%

The Mortality Risk and Pulmonary Fibrosis Investigated by Time-Resolved Fluorescence Spectroscopy from Plasma in COVID-19 Patients

Wybranowski

Pyskir

Bosek

et al. 2022

JCM

Self Cite

View full text Add to dashboard Cite

A method of rapidly pointing out the risk of developing persistent pulmonary fibrosis from a sample of blood is extraordinarily needed for diagnosis, prediction of death, and post-infection prognosis assessment. Collagen scar formation has been found to play an important role in the lung remodeling following SARS-CoV-2 infection. For this reason, the concentration of collagen degradation products in plasma may reflect the process of lung remodeling and determine the extent of fibrosis. According to our previously published results of an in vitro study, an increase in the concentration of type III collagen degradation products in plasma resulted in a decrease in the fluorescence lifetime of plasma at a wavelength of 450 nm. The aim of this study was to use time-resolved fluorescence spectroscopy to assess pulmonary fibrosis, and to find out if the lifetime of plasma fluorescence is shortened in patients with COVID-19. The presented study is thus far the only one to explore the fluorescence lifetime of plasma in patients with COVID-19 and pulmonary fibrosis. The time-resolved spectrometer Life Spec II with the sub-nanosecond pulsed 360 nm EPLED® diode was used in order to measure the fluorescence lifetime of plasma. The survival analysis showed that COVID-19 mortality was associated with a decreased mean fluorescence lifetime of plasma. The AUC of mean fluorescence lifetime in predicting death was 0.853 (95% CI 0.735–0.972, p < 0.001) with a cut-off value of 7 ns, and with 62% sensitivity and 100% specificity. We observed a significant decrease in the mean fluorescence lifetime in COVID-19 non-survivors (p < 0.001), in bacterial pneumonia patients without COVID-19 (p < 0.001), and in patients diagnosed with idiopathic pulmonary fibrosis (p < 0.001), relative to healthy subjects. Furthermore, these results suggest that the development of pulmonary fibrosis may be a real and serious problem in former COVID-19 patients in the future. A reduction in the mean fluorescence lifetime of plasma was observed in many patients 6 months after discharge. On the basis of these data, it can be concluded that a decrease in the mean fluorescence lifetime of plasma at 450 nm may be a risk factor for mortality, and probably also for pulmonary fibrosis in hospitalized COVID-19 patients.

show abstract

Use of time-resolved fluorescence spectroscopy to evaluate diagnostic value of collagen degradation products

Cited by 5 publications

References 45 publications

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

A study of the oxidative processes in human plasma by time-resolved fluorescence spectroscopy

The Mortality Risk and Pulmonary Fibrosis Investigated by Time-Resolved Fluorescence Spectroscopy from Plasma in COVID-19 Patients

Contact Info

Product

Resources

About