Raman study of the shockwave effect on collagens

Cárcamo-Vega, José J.; Aliaga, Álvaro; Clavijo, R. E.; Brañes, Manuel; Campos‐Vallette, Marcelo

doi:10.1016/j.saa.2011.10.049

Cited by 44 publications

(40 citation statements)

References 19 publications

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“…In this work, Raman spectra of solid COLL from two different origins (from a rat tail and bovine tendon) have been recorded. It has been previously shown that structures and, therefore, Raman spectra of bovine COLL types I and II are similar to the spectrum of COLL type I from rats . This similarity was also observed during our studies at all excitation wavelengths; therefore, only spectra for COLL from a rat tail are presented in Figs.…”

Section: Resultssupporting

confidence: 86%

“…Spectra in this work are in agreement with previously obtained data and show amide I and III bands at ca . 1670 and 1271 cm −1 , respectively . The difference in the relative intensity of the amide bands in the spectra obtained with various laser excitations is observed, i.e.…”

Section: Resultsmentioning

confidence: 83%

“…The COLL Raman spectrum was described already in 1975, and since then literature in the subject has been rapidly developing. Among others, issues such as temperature dependence of COLL spectra, hydration processes, shockwave effects on COLL structure and dependence of COLL fibrils orientation on Raman spectra have been investigated. Raman spectroscopy was also successfully applied to investigate COLL in biological samples …”

Section: Resultsmentioning

confidence: 99%

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Raman spectroscopy of proteins: a review

Ryguła

Majzner

Marzec

et al. 2013

J Raman Spectroscopy

867

790

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In this work, 26 proteins of different structure, function and properties are investigated by Raman spectroscopy with 488, 532 and 1064 nm laser lines. The excitation lines were chosen in NIR and Vis range as the most common and to show the difference due to normal and resonance effect, sometimes accompanied by the fluorescence. The selected proteins were divided, according to the Structural Classification of Proteins, into four classes according to their secondary structure, i.e. α‐helical (α), β‐sheet (β), mixed structures (α/β, α + β, s) and others. For all compounds, FT‐Raman and two Vis spectra are presented along with the detailed band assignment. To the best of our knowledge, this is the first review showing the potential of Raman spectroscopy for the measurement and analysis of such a large collection of individual proteins. This work can serve as a comprehensive vibrational spectra library, based on our and previous Raman measurements. Copyright © 2013 John Wiley & Sons, Ltd.

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Section: Resultssupporting

confidence: 86%

Section: Resultsmentioning

confidence: 83%

Section: Resultsmentioning

confidence: 99%

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Raman spectroscopy of proteins: a review

Ryguła

Majzner

Marzec

et al. 2013

J Raman Spectroscopy

867

790

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“…A, spectrum 2). The characteristic Raman spectrum of collagen exhibits two intense band doublets centered at ~860 cm ‐1 and ~940 cm ‐1 that are associated with proline and protein backbone vibrational modes, as well as an intense, broad amide III band at ~1260 cm ‐1 . Molecular assignments for all the major Raman spectroscopic peaks observed in this work are presented in Table .…”

Section: Resultsmentioning

confidence: 75%

Confocal Raman microspectroscopy discriminates live human metastatic melanoma and skin fibroblast cells

Terentis

Fox

Friedman

et al. 2013

J Raman Spectroscopy

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Confocal Raman microspectroscopy (CRM) continues to develop as a promising technique with possible clinical applications for the diagnosis and treatment of skin cancers. CRM studies of single cells can provide information on the biochemical content of cancer cells in situ, potentially providing new biochemical signatures or markers of cancer cells. Here, we report a CRM study of single, living human metastatic melanoma cells (SK‐Mel‐2) and normal skin fibroblast cells (BJ) cultured and examined under identical experimental conditions. A total of almost 1200 Raman spectra were measured from more than 120 BJ and SK‐Mel‐2 cells using an inverted microscope with 647 nm laser excitation. Raman spectra were measured from within three distinct intracellular regions of the cells – cytoplasm, nucleoplasm, and nucleolus. When Raman spectra from each cell type were compared using principal components analysis (PCA) and linear discriminant analysis with leave‐one‐dish‐out cross‐validation (LDA‐CV), the two cell types were discriminated with 93% (cytoplasm), 98% (nucleolus), and 96% (nucleoplasm) accuracy. The main biochemical differences identified between the two cell types were higher RNA levels in the nucleoli of BJ cells and high amounts of lipid and collagen in the cytoplasm of SK‐Mel‐2 cells. For both cell types, higher levels of RNA were detected in the nucleoli versus the nucleoplasm. PCA with LDA‐CV was 98% (cytoplasm), 93% (nucleoplasm), and 73% (nucleolus) accurate in identifying the intracellular region based on the Raman spectra from both cell types. No significant trend was observed when the data were analyzed with respect to cell passage number. Thus, CRM with PCA and LDA‐CV successfully discriminated two skin cancer‐relevant cell lines while detecting different amounts of nucleic acids, lipids, and proteins in distinct intracellular regions, further underscoring its potential as a clinical diagnostic tool. Copyright © 2013 John Wiley & Sons, Ltd.

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“…8). A partir de trabajos previos en el análisis vibracional Raman sobre compuestos orgánicos y sistemas biológicos (Cárcamo et al 2012a(Cárcamo et al , 2012b, así como de datos publicados (Frost et al 2008;Vandenabeele et al 2000), podemos proponer la presencia de oxalatos y material proteico en la mezcla pictórica. Como se muestra en la línea superior, la existencia de oxalatos puede ser inferida por la observación de las bandas ubicadas a 1465 y 1497 cm -1 , mientras que en la línea inferior podemos atribuir las bandas a1665, 1526 y 1292 cm -1 a los modos de vibración amida i, amida ii y amida iii, respectivamente, correspondientes a la estructura secundaria de proteínas.…”

Section: Resultsunclassified