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Measurement of bacterial concentration fractions in polymicrobial mixtures by Raman microspectroscopy.

Relative concentrations of Streptococcus mutans and Streptococcus sanguis are important parameters in the study of dental caries, but current methods of measuring these concentrations are time consuming and prone to inaccuracies. We investigate the use of Raman spectroscopy for measuring relative concentrations of these two bacterial species in solid mixtures. To our knowledge, this is the first time Raman spectroscopy has been used to analyze bacterial mixtures rather than to identify the species of a pure colony. Mixtures of the two streptococcal species in various ratios are measured for 200 s using a home-built Raman microscope. Spectral correlations with bacterial content were identified via partial least-squares analysis. The relative concentrations of S. mutans in subsequent samples are predicted with a root mean squared error below 5%. In clinical plaque samples, this sort of accuracy would enable discrimination between normal and dangerously elevated levels of S. mutans. Samples with and without salivary proteins are predicted with equal accuracy. This result shows the potential of Raman spectroscopy for analyzing mixed populations of bacteria, such as those that occur in oral plaques.

Algorithms↗
PubMed2005

Potential of NIR-FT-Raman spectroscopy in natural carotenoid analysis.

This paper demonstrates the special advantages of FT-Raman spectroscopy for in situ studies of several carotenoids that occur ubiquitously in the plant kingdom. Spectra obtained from various tissues of a range of plant species indicate that the wavenumber location of C=C stretching vibrations is mainly influenced both by the length as well as by the terminal substituents of the polyene chain of carotenoids and by their interaction with other plant constituents. The obtained results show also the usefulness of Raman spectroscopy in the investigation of cis-trans isomerization of carotenoids during processing. Additionally, 2-D Raman mappings present a unique possibility to evaluate the individual distribution of carotenoids in the intact plant tissue; in this context different 7-, 8-, and 9-double bond conjugated carotenoids can be analyzed independently in the same sample. Furthermore, the use of Raman spectroscopy for in situ detection of unstable substances such as epoxycarotenoids is discussed.

Carotenoids↗
PubMed2003

Studies on the interaction between Ag(+) and human serum albumin.

The interaction between Ag(+) and human serum albumin (HSA) has been intensively studied by means of equilibrium dialysis, ligand-to-metal charge transition (LMCT) bands, circular dichroism (CD) and Raman spectroscopy. Scatchard analysis of the results of equilibrium dialysis indicates the presence of two types of binding sites for Ag(+) on HSA, and the orders of magnitude of binding stability constants are found to be 10(5) and 10(4), respectively. During the binding process, a gradual increase in absorbance values of LMCT bands is observed with time-scanning UV absorption spectra, implying the Ag(I) centers are continually formed in HSA. The time-scanning CD spectra provide evidence that the binding of Ag(+) induces HSA to undergo a slow rearrangement of tertiary structure, and to change from the original conformation in the absence of Ag(+) (B-state) to conformation binding with Ag(+) (A-state). The rate constants and activation free energy of A-B transition are calculated. The Raman spectrum of Ag(I)-HSA system shows distinct vibration bands at 224 and 246 cm(-1) in the low-frequency region, which significantly reveal the formation of Ag-S and Ag-N bonds. In addition, the electrostatic interaction between Ag(+) and negatively charged oxygen is also detected with Raman spectroscopy.

Binding Sites↗
PubMed2005

Characterization of different laser irradiation methods for quantitative Raman tablet assessment.

Quantitative Raman spectroscopy of conventional wet granulated pharmaceutical immediate release tablets and subsequent data evaluation was investigated. Different aspects of quantitative assessment of active pharmaceutical ingredient (API) in intact tablets with special focus on sub-sampling issues were addressed. Four different geometric laser irradiance patterns were examined to study the effect of sub-sampling within the tablets. The Raman data was evaluated using both univariate and multivariate techniques. UV absorbance spectroscopy was used as a reference method. The best result in terms of prediction error was attained by irradiating a large area of the tablets. Using multivariate calibration with multiplicative signal correction (MSC) the prediction error was 1.7%. In addition, the effect of tablet density on the Raman assessment was investigated. It was found that quantitative Raman assessment of chemical content can be made insensitive to variations in tablet density corresponding to a manufacturing compression interval of 5-20 kN provided that adequate data treatment is used. A short discussion about sample heating in the context of different irradiation patterns is included with reference to previous work. In conclusion, the present study provides a platform for developing an implementation strategy for quantitative Raman spectroscopy for both laboratory analysis and process analytical technology (PAT) applications.

Calibration↗
PubMed2003

Raman structural markers of tryptophan and histidine side chains in proteins.

The Raman spectrum of a protein contains a wealth of information on the structure and interaction of the protein. To extract the structural information from the Raman spectrum, it is necessary to identify and interpret the marker bands that reflect the structure and interaction in the protein. Recently, new Raman structural markers have been proposed for the tryptophan and histidine side chains by examining the spectra-structure correlations of model compounds. Raman structural markers are now available for the conformation, hydrogen bonding, hydrophobic interaction, and cation-pi interaction of the indole ring of Trp. For His, protonation, tautomerism, and metal coordination of the imidazole ring can be studied by using Raman markers. The high-resolution X-ray crystal structures of proteins provide the basis for testing and modifying the Raman structural markers of Trp and His. The structures derived from Raman spectra are generally consistent with the X-ray crystal structures, giving support for the applicability of most Raman structural makers. Possible modifications and limitations to some marker bands are also discussed.

Cations↗
PubMed2004

Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins.

A new deep-UV Raman spectrometer utilizing a laser source tunable between 193 and 205 nm has been designed, built, and characterized. Only selected wavelengths from this range have previously been accessible, by Raman shifting of the second, third, and fourth harmonics of the Nd:YAG fundamental in hydrogen. The apparatus was demonstrated to be a useful tool for characterizing hen egg white lysozyme structural rearrangements at various stages of fibril formation. High-quality deep-UV resonance Raman spectra were obtained for both a protein solution and a highly-scattering gelatinous phase formed by fibrillogenic species. In addition to amide bands, strong contribution of nu(12) and ring-C phenylalanine vibrational modes was observed at excitation wavelengths below 200 nm. Remarkably, the Raman cross-section of these modes revealed dramatic change of lysozyme in response to heat denaturation and fibril formation. These results indicate that phenylalanine could serve as a new deep-UV Raman probe of protein structure.

Molecular Probes↗
PubMed1987

Phenylhydrazine as probe for cofactor identification in amine oxidoreductases. Evidence for PQQ as the cofactor in methylamine dehydrogenase.

Homogeneous methylamine dehydrogenase (primary-amine:(acceptor) oxidoreductase (deaminating), EC 1.4.99.3, MADH) from the bacterium Thiobacillus versutus was treated with the inhibitor phenylhydrazine (PH). Derivatization of the cofactor in MADH took place in a fast reaction to give compound I. A different product, compound II, was formed in a slow reaction at high O2 concentrations. The compounds I and II could be removed from the protein by proteolysis with pronase and purified to homogeneity. Products showing identical absorption spectra and chromatographic behaviour were isolated from the reaction mixture after incubating pyrroloquinoline quinone (PQQ) with PH. Upon dissolving in dimethyl sulphoxide, both the enzyme-derived as well as the model-system-derived compounds I and II were nearly quantitatively transformed into PQQ. The conclusion is, therefore, that MADH from T. versutus contains covalently bound PQQ, removable from the protein with pronase, and not a structural analogue of this cofactor without the carboxylic acid groups, as was recently proposed for MADH from Bacterium W3A1 [(1986) Biochem. Biophys. Res. Commun. 141, 562-568]. The properties of compounds I and II suggest that they are the 'azo adduct' and the 'hydrazone adduct' of PH and PQQ at the C(5)-position, respectively. The finding that the reaction of a hydrazine with PQQ can lead to two different products, in enzymes as well as in a model system, has important implications for the interpretation of recent comparative studies aimed at detection of PQQ in amine oxidoreductases with Raman spectroscopy.

Oxidoreductases Acting on CH-NH Group Donors↗
PubMed1991

Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy.

Previous work by Wishart et al. (in press) and others [(1989) J. Magn. Reson. 83, 441-449; (1990) J. Magn. Reson. 90, 165-176] has shown a strong tendency for protein secondary structure to be manifested in 1H NMR chemical shifts. Based on these earlier results, two techniques have been developed for the quantification of secondary structure in proteins. Both methods allow for the rapid and accurate determination of the percent content of helix, coil, and beta-strand based on the integration (or peak enumeration) of selected portions of either 1-D or 2-D 1H NMR spectra. These new and very simple procedures have been found to compare quite favorably to other well established techniques for secondary structure determination such as CD, Raman and IR spectroscopy.

Animals↗