Surface enhanced Raman scattering for robust, sensitive detection and confirmatory identification of dried bloodstains

Shaine, M. L.; Premasiri, W. Ranjith; Ingraham, H.; Andino, Richard S.; Lemler, Paul M.; Brodeur, Amy N.; Ziegler, L. D.

doi:10.1039/d0an01132k

Cited by 23 publications

(37 citation statements)

References 67 publications

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“…In recent work focused on developing a SERS-based protocol for forensically relevant rapid detection and identification of trace amounts of human body fluids, we noted the dramatic difference between the 785-nm excited SERS signature of dried bloodstains on Au and Ag substrates. [29] This observed characteristic SERS dried blood spectrum is due to a ferric, high spin PPIX moiety resulting from the denatured hemoglobin protein and is nearly identical to the observed 785-nm SERS spectrum of hematin. [29] This excitation wavelength is far off resonance with the well-known π-π* porphyrin-based electronic transitions; and thus, unlike most of the previous SERS spectra of hemelike proteins, [30][31][32][33][34][35][36] these robust, strongly enhanced (enhancement factor [EF] ≥ 10 9 ) spectra are not SERRS spectra.…”

Section: Introductionsupporting

confidence: 59%

“…[ 29 ] This observed characteristic SERS dried blood spectrum is due to a ferric, high spin PPIX moiety resulting from the denatured hemoglobin protein and is nearly identical to the observed 785‐nm SERS spectrum of hematin. [ 29 ] This excitation wavelength is far off resonance with the well‐known π–π* porphyrin‐based electronic transitions; and thus, unlike most of the previous SERS spectra of hemelike proteins, [ 30–36 ] these robust, strongly enhanced (enhancement factor [EF] ≥ 10 9 ) spectra are not SERRS spectra. Some previous SERS studies, particularly of analytes with thiol substituents, have resulted from chemical reactivity resulting in valence bond formation, such as H atom dissociation and direct S attachment to Au or Ag surfaces.…”

Section: Introductionmentioning

confidence: 63%

“…Oxyhemoglobin was prepared as described previously. [ 29 ] Manganese PPIX chloride (Mn(III) PPIX Cl), cobalt PPIX chloride (Co(III) PPIX Cl), and hematin (Fe(III) PPIX IX OH) were used as purchased from Sigma‐Aldrich. Although of sufficient quality for SERS acquisition, purchased PPIX (Sigma‐Aldrich 95%) required additional purification for NR observations at 785 nm.…”

Section: Methodsmentioning

confidence: 99%

“…The details of this synthetic procedure and the characterization of their performance for providing reproducible SERS spectra for a range of biomedical applications have been described in prior publications. [29,[63][64][65]…”

Section: Sers Substratesmentioning

confidence: 99%

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Chemical enhancement effects on protoporphyrin IX surface‐enhanced Raman spectra: Metal substrate dependence and a vibronic theory analysis

McNeely

Ingraham

Premasiri

et al. 2020

J Raman Spectroscopy

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Surface‐enhanced Raman spectra (SERS) of protoporphyrin IX (PPIX) and analogous metal‐containing PPIX compounds excited at 785 nm exhibit robust, strongly enhanced (~5 × 109) spectra that are highly dependent on the nanostructured metal (Au or Ag). Although the relative intensities of the 785‐nm SERS vibrational spectral features are very similar for all observed PPIX‐based compounds, the relative intensities are dramatically different on Au and Ag SERS substrates. Time‐dependent density functional theory (TDDFT) calculations are carried out for Au2/Ag2–PPIX complexes to understand the origins of this chemical enhancement contribution to the observed SERS spectra. The observed metal dependence of the SERS spectra in the heme ring stretching region (1,500–1,620 cm−1) are reproduced by calculated resonance Raman intensities due to low‐lying metal (σ) to molecule (π*) charge transfer excitations of the metal dimer–PPIX complexes when the metal dimer is near a porphyrin ring Cβ position. The nuclear coordinate dependence of electronic transition moments is essential for capturing the effects of these CT excitations. A simple method for determining the importance of the transition moment normal mode dependence relative to Franck–Condon factors (A term) is described and implemented. The consequences of this vibronic analysis for the observation of overtone/combination bands in SERS spectra are discussed.

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Section: Introductionsupporting

confidence: 59%

Section: Introductionmentioning

confidence: 63%

Section: Methodsmentioning

confidence: 99%

Section: Sers Substratesmentioning

confidence: 99%

See 2 more Smart Citations

Chemical enhancement effects on protoporphyrin IX surface‐enhanced Raman spectra: Metal substrate dependence and a vibronic theory analysis

McNeely

Ingraham

Premasiri

et al. 2020

J Raman Spectroscopy

Self Cite

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show abstract

“…It was previously established for hemoglobin at least, that the 785‐nm SERS spectrum in 50% acetic acid on Au and on Ag substrates have distinct patterns of relative intensities due, in part, to the metal specificity of 785‐nm chemical enhancement effects. [ 28,32 ] The studies describe here will address whether such metal surface dependent differences extend to all the heme proteins and solvent environments observed here.…”

Section: Introductionmentioning

confidence: 95%

NIR surface enhanced Raman spectra of biological hemes: Solvation and plasmonic metal effects

Ingraham

Premasiri

Ziegler

2021

J Raman Spectroscopy

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Surface enhanced Raman spectra (SERS) excited at 785 nm are reported for hemoglobin, myoglobin, two heme B proteins, and cytochrome c, a heme C protein, solubilized in a variety of solvent systems and then placed on Au and Ag substrates. These solvent environments include H2O pH 7.4, HCl/water pH 2, HCl/50% ethanol pH 2, 50% acetic acid and the organic layer of a pH 2 HCl/butanone mixture. To obtain the most intense SERS spectra of heme B proteins (Mb and Hb) it is not sufficient to be in a low pH (pH ~ 2) denaturing environment. A hydrophobic solvent component is additionally required in order to efficiently solubilize the cleaved heme moiety and consequently observe intense SERS spectra indicative of these heme B proteins. Although both heme B proteins exhibit virtually identical, metal (Au, Ag) specific SERS spectra, Cyt c is much weaker in the low pH environments and only displays a Ag‐like SERS spectrum on both metals indicating that this heme C protein is not cleaved in any of these solvation environments. The strong SERS signals of hemoglobin and myoglobin are due to hemin and ferric acetate heme formed in pH 2 HCl/ethanol and pH 2/50% acetic acid solutions respectively. SERS vibrational features confirm oxidation state, coordination number and ligands. SERS signals due to globin protein aggregation effects are reduced in low pH solvent systems with polarities lower than pure water. These results confirm the mechanism of a successful acetic acid protocol previously developed for the highly sensitive SERS detection of dried blood for forensic applications and indicate how it may be further improved to achieve even higher SERS sensitivity for heme protein detection.

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The key role of ergothioneine in label‐free surface‐enhanced Raman scattering spectra of biofluids: a retrospective re‐assessment of the literature

Fornasaro

Sergo

2022

FEBS Letters

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Label-free surface-enhanced Raman scattering (SERS) has recently gained attention in the field of liquid biopsy as a rapid and relatively inexpensive technique that could significantly ease clinical diagnosis and prognosis by investigating a biofluid sample with a laser. Indeed, SERS spectra provide information about a set of metabolites present in the analysed biofluid, thereby offering biochemical insight into specific health conditions. Ergothioneine plays a key role since it is one of the few metabolites in biofluids that are detectable by label-free SERS. In the past decade, many studies characterizing biofluids or other biological samples have unknowingly linked this amino acid with crucial metabolic processes, including inflammation, in a plethora of diseases. However, since the SERS spectrum of ergothioneine has been reported only recently, most past studies inadvertently assigned what are now recognized as the spectral features of this compound to other molecules. The purpose of the present review is to summarize and re-evaluate these studies in the light of the recent SERS characterization of ergothioneine so as to better recognize the role of ergothioneine in many clinical conditions.

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Surface enhanced Raman scattering for robust, sensitive detection and confirmatory identification of dried bloodstains

Abstract: An optimized procedure is described for the acquisition of 785 nm excited SERS spectra of dried bloodstains and shown to offer great potential for rapid, portable, highly sensitive and specific,...

Cited by 23 publications

References 67 publications

Chemical enhancement effects on protoporphyrin IX surface‐enhanced Raman spectra: Metal substrate dependence and a vibronic theory analysis

Chemical enhancement effects on protoporphyrin IX surface‐enhanced Raman spectra: Metal substrate dependence and a vibronic theory analysis

NIR surface enhanced Raman spectra of biological hemes: Solvation and plasmonic metal effects

The key role of ergothioneine in label‐free surface‐enhanced Raman scattering spectra of biofluids: a retrospective re‐assessment of the literature

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