Surface-enhanced Raman spectroscopy of free and complexed bilirubin

Hsieh, You Zung.; Lee, Nam Soo; Sheng, Rong Sheng.; Morris, Michael D.

doi:10.1021/la00078a047

Cited by 21 publications

(11 citation statements)

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“…Fatty acids such as bees wax have medium to strong bands around 1130 + 5 and 1300 + 5 cm 21 , and very strong bands between 2800 and 3000 cm 21 [66,71]. Tetrapyrroles, such as bilirubin, exhibit a prominent band between 1610 and 1620 cm 21 attributed to C¼C stretching [72,73].…”

Section: Other Compoundsmentioning

confidence: 99%

“…saffron) also have a very strong band at 1600 + 10 cm 21 [66,67] , and very strong bands between 2800 and 3000 cm 21 [66,71]. Tetrapyrroles, such as bilirubin, exhibit a prominent band between 1610 and 1620 cm 21 attributed to C¼C stretching [72,73]. In contrast to the above listed compounds, many of the band positions in the spheniscin spectrum exactly match the porphyrin marker bands in cytochrome c' (i.e.…”

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confidence: 94%

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Vibrational spectroscopic analyses of unique yellow feather pigments (spheniscins) in penguins

Thomas

McGoverin

McGraw

et al. 2013

J. R. Soc. Interface.

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Many animals extract, synthesize and refine chemicals for colour display, where a range of compounds and structures can produce a diverse colour palette. Feather colours, for example, span the visible spectrum and mostly result from pigments in five chemical classes (carotenoids, melanins, porphyrins, psittacofulvins and metal oxides). However, the pigment that generates the yellow colour of penguin feathers appears to represent a sixth, poorly characterized class of feather pigments. This pigment class, here termed 'spheniscin', is displayed by half of the living penguin genera; the larger and richer colour displays of the pigment are highly attractive. Using Raman and mid-infrared spectroscopies, we analysed yellow feathers from two penguin species (king penguin, Aptenodytes patagonicus; macaroni penguin, Eudyptes chrysolophus) to further characterize spheniscin pigments. The Raman spectrum of spheniscin is distinct from spectra of other feather pigments and exhibits 17 distinctive spectral bands between 300 and 1700 cm 21 . Spectral bands from the yellow pigment are assigned to aromatically bound carbon atoms, and to skeletal modes in an aromatic, heterocyclic ring. It has been suggested that the penguin pigment is a pterin compound; Raman spectra from yellow penguin feathers are broadly consistent with previously reported pterin spectra, although we have not matched it to any known compound. Raman spectroscopy can provide a rapid and non-destructive method for surveying the distribution of different classes of feather pigments in the avian family tree, and for correlating the chemistry of spheniscin with compounds analysed elsewhere. We suggest that the sixth class of feather pigments may have evolved in a stem-lineage penguin and endowed modern penguins with a costly plumage trait that appears to be chemically unique among birds.

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Section: Other Compoundsmentioning

confidence: 99%

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confidence: 94%

Vibrational spectroscopic analyses of unique yellow feather pigments (spheniscins) in penguins

Thomas

McGoverin

McGraw

et al. 2013

J. R. Soc. Interface.

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“…Therefore, the Raman bands at 1616, 1577 and 1562 cm -1 involved in C=C bonds exhibit a red shift, and the 1497 cm -1 band, C-C bonds of lactams and pyrroles, blue-shift in the aggregate of the BR-BSA complex. These changes are possibly concomitant with ruptures of the internal hydrogen bonds between the propionate groups and the pyrromethenone rings, 11 and the hybrid of the lactam groups of 844 ANALYTICAL SCIENCES JULY 2007, VOL. 23 BR induced by protonated amino groups in BSA.…”

Section: Resonance Raman Spectra Of the Aggregate Of The Br-bsa Complmentioning

confidence: 99%

“…If the body does not produce an adequate amount of albumin, BR is sequestered directly under the skin, and even provoke BR encephalopathy by passing the blood-brain barrier and penetrating the phospholipid membrane of neurons. Although BR and its complex with serum albumin (SA) have been extensively investigated in bulk phases, [2][3][4][5][6][7][8][9][10][11] the complexation of BR with SA has never been studied at a liquid/liquid interface, which is recognized as being a model of a biological membrane, 12 and as a specific reaction field in the solvent extraction of metal ions. 13 In the present work, resonance Raman spectroscopy was applied to measure the microenvironment of an interfacial complex of BR with bovine serum albumin (BSA) and the aggregate of the complex at the organic/water interface.…”

Section: Introductionmentioning

confidence: 99%

Resonance Raman Spectroscopic Study on Chiral Aggregation of Bilirubin-Bovine Serum Albumin Complex Formed at Liquid/Liquid Interface

Yin

Watarai

2007

ANAL. SCI.

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Resonance Raman spectroscopy assisted by centrifugal liquid membrane/circular dichroism (CLM-CD) and UV/Vis absorption spectroscopies was applied to measure the binding state of bilirubin (BR) in the complex with bovine serum albumin (BSA) formed at a heptane/water interface. The bisignate Cotton effects in the interfacial CD spectra and the red shift and linewidth increase of the BR absorption band around 450 nm indicated the formation of the BR-BSA complex at the interface and the chiral conversion of BR molecules in the aggregates. The resonance Raman spectra of BR observed at the interface suggested that the interfacial BR-BSA complex formed during the initial 15 min after the contact of the two phases had a similar structure with that in solution, but after 15 min were forming aggregates coexisting with solid micro-particles. These experimental results strongly suggested that the chiral interconversion of BR from (P+) conformation to (M-) conformation in the interfacial complex was accompanied by aggregation of the BR-BSA complexes. In the present study, resonance Raman microscopic spectrometry was proved to be highly useful for characterizing the solid like aggregate formed at the liquid/liquid interface. 3 The dashed lines show intramolecular hydrogen bondings that link the dipyrrinones to opposing propionic acids. θ denotes the dihedral angle (see the text for details).

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“…Resonance Raman microspectroscopy has also been proposed as a diagnostic for bilirubin gallstones [4, 51. Resonance Raman spectroscopy has been used to study changes in intramolecular hydrogen bonding in the bilirubin-albumin complex [6] and in bilirubin phospholipid complexes [7]. Even surface-enhanced Raman spectroscopy has been applied to the bilirubin-albumin complex system [8].…”

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confidence: 99%

Normal coordinate analysis of bilirubin vibrational spectra: Effects of intramolecular hydrogen bonding

Yang¹,

Taylor²,

Morris³

et al. 1993

Spectrochimica Acta Part A: Molecular Spectroscopy

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Ah&act-Normal coordinate analyses are presented for half-bilirnbin molecules. Calculations for the A-B pyrromethenone include intramolecular hydrogen bonds, while those for the C-D chromophore exclude intramolecular hydrogen bonds. Valence force-held parameters have been optimized to correlate closely with the IR and Raman spectra of the target molecules. The results of the calculations are compared with the spectra of bilirnbin IXa and various model compounds in the solid state and solution.

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Surface-enhanced Raman spectroscopy of free and complexed bilirubin

Cited by 21 publications

References 0 publications

Vibrational spectroscopic analyses of unique yellow feather pigments (spheniscins) in penguins

Vibrational spectroscopic analyses of unique yellow feather pigments (spheniscins) in penguins

Resonance Raman Spectroscopic Study on Chiral Aggregation of Bilirubin-Bovine Serum Albumin Complex Formed at Liquid/Liquid Interface

Normal coordinate analysis of bilirubin vibrational spectra: Effects of intramolecular hydrogen bonding

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