2013
DOI: 10.1007/s10895-013-1335-2
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Native Fluorescence and Time Resolved Fluorescence Spectroscopic Characterization of Normal and Malignant Oral Tissues Under UV Excitation—an In Vitro Study

Abstract: The present work aims to investigates the native fluorescence and time resolved fluorescence spectroscopic characterization of oral tissues under UV excitation. The fluorescence emission spectra of oral tissues at 280 nm excitation were obtained. From the spectra, it was observed that the alteration in the biochemical and morphological changes present in tissues. Subsequently, the Full width at Half Maximum (FWHM) of every individual spectra of 20 normal and 40 malignant subjects were calculated. The student's… Show more

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Cited by 17 publications
(16 citation statements)
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“…42 Where i represents pre-exponential factors, 2 indicates goodness of fit. The emission decay curves of HfO 2 NPs were measured monitoring the emission at 350 and 430 nm at the excitation wavelength of 280 nm (Figs.…”
Section: Lifetime Analysismentioning
confidence: 99%
“…42 Where i represents pre-exponential factors, 2 indicates goodness of fit. The emission decay curves of HfO 2 NPs were measured monitoring the emission at 350 and 430 nm at the excitation wavelength of 280 nm (Figs.…”
Section: Lifetime Analysismentioning
confidence: 99%
“…Optical spectroscopy plays an important role in the development of non‐invasive detection methods in the diagnosis of various cancers viz., oral, breast, lung, cervix, skin, bladder, esophagus, laryngeal, prostate cancers, etc. Extensive studies have been made on the use of native fluorescence spectroscopy in the discrimination of cancer from normal subjects . Although fluorescence technique is simple and sensitive, it has the following limitations, multiple wavelengths of excitation is required to study the fluorophores present in tissue and because of this, there is a possibility of photobleaching of the native fluorophores.…”
Section: Introductionmentioning
confidence: 99%
“…The observed differences in fast, intermediate, and slow lifetime component could be due to the presence of different microenvironment such as viscosity and chromophores of charged group accomplished by tryptophan residues in proteins [ 20 , 31 ]. It was reported that single tryptophan and its residues conformers itself were strongly influenced by their microenvironment; hence conformational changes may result in changes over lifetime [ 32 ].…”
Section: Resultsmentioning
confidence: 99%