Fourier transform Raman approach to structural correlation in hemoglobin derivatives

Venkatesh, Balan; Ramasamy, Somasundaram; Mylrajan, M.; Asokan, Rengasamy; Manoharan, P. T.; Rifkind, Joseph M.

doi:10.1016/s1386-1425(99)00008-6

Cited by 34 publications

(42 citation statements)

References 26 publications

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“…Based on our previous FT-Raman experiments, we considered the bands at 1657 and 1574 cm Ϫ1 as the 4-and 5-coordinate marker bands in NiHb, respectively. 21 The 4-coordination marker bands corre-sponding to 1379, 1593, and 1660 cm Ϫ1 arising from FT-Raman experiments of our work ( Figure 4e) are in good correspondence with the work of Shelnutt and coworkers 15 using 406.7-nm resonance Raman excitation. However, the low intensity bands found at 1580 cm Ϫ1 in 4e, the type of which was not found at all in the work of Shelnutt and coworkers, must have come from some other local vibrations caused by FT-Raman excitation.…”

Section: Ft-raman Studiessupporting

confidence: 88%

Studies on heme release from normal and metal ion reconstituted hemoglobin mediated through ionic surfactant

Venkatesh

Santhanalakshmi

et al. 2004

Biopolymers

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The interaction of metal-substituted hemoglobin (MHb), where M = Ni and Cu (T-state with no O2 and CO binding capability) and Fe (R-state when CO is bound), with cationic cityl trimethyl ammonium bromide (CTAB) and anionic (sodium dodecyl sulfate-SDS) surfactants has been studied using spectroscopic techniques-UV-visible, electron paramagnetic resonance (EPR), and Fourier transform-Raman-with additional supportive evidence coming from conductivity measurements. We observed the loss of 5-coordination in all three hemoglobins below the critical micelle concentration (CMC) of surfactant, with noticeable differences, suggesting differing mechanisms involved in this process. In addition, above the CMC, Ni- and Cu-hemes were found to leave their proteins more easily than Fe-heme, presumably due to weaker or no bond with the proximal histidine in the former. The released heme is stabilized by micellar media through a hydrophobic interaction process. Of the two surfactants, CTAB seems to be capable of releasing the heme better than SDS and it is attributed to the greater hydrophobicity of CTAB though the charge of the surfactant plays an important role.

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Section: Ft-raman Studiessupporting

confidence: 88%

Studies on heme release from normal and metal ion reconstituted hemoglobin mediated through ionic surfactant

Venkatesh

Santhanalakshmi

et al. 2004

Biopolymers

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“…The vibrational bands observed in this normal Raman spectrum are nearly identical to the previously reported non-SERS spectra of whole human blood excited by near IR radiation (720nm or 830 nm). 14, 31, 42, 45 Furthermore, comparison with previous Raman studies of oxygenated and deoxygenated single RBCs 39 and hemoglobin, 40 reveal that the most significant differences between the dried and liquid whole blood Raman spectra excited at 785 nm (Fig. 1) are due to the state of hemoglobin oxygenation.…”

Section: Resultsmentioning

confidence: 54%

Surface-Enhanced Raman Scattering of Whole Human Blood, Blood Plasma, and Red Blood Cells: Cellular Processes and Bioanalytical Sensing

2012

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SERS spectra of whole human blood, blood plasma, and red blood cells on Au nanoparticle SiO 2 substrates excited at 785 nm have been observed. For the sample preparation procedure employed here, the SERS spectrum of whole blood arises from the blood plasma component only. This is in contrast to the normal Raman spectrum of whole blood excited at 785 nm and open to ambient air, which is exclusively due to the scattering of oxyhemoglobin. The SERS spectrum of whole blood shows a storage time dependence that is not evident in the non-SERS Raman spectrum of whole blood. Hypoxanthine, a product of purine degradation, dominates the SERS spectrum of blood after ∼10−20 h of storage at 8 °C. The corresponding SERS spectrum of plasma isolated from the stored blood shows the same temporal release of hypoxanthine. Thus, blood cellular components (red blood cells, white blood cells, and/or platelets) are releasing hypoxanthine into the plasma over this time interval. The SERS spectrum of red blood cells (RBCs) excited at 785 nm is reported for the first time and exhibits well-known heme group marker bands as well as other bands that may be attributed to cell membrane components or protein denaturation contributions. SERS, as well as normal Raman spectra, of oxy-and met-RBCs are reported and compared. These SERS results can have significant impact in the area of clinical diagnostics, blood supply management, and forensics.

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“…The component dominated by the fluorescent background was important only for fitting purposes, so the two other components were named as component 1 (hemoglobindominated) and component 2 (fibrin-dominated). Component 1 was assigned to hemoglobin and its derivatives due to the presence of peaks at 1000, 1368, 1542 and 1620 cm -1 (Figure 1.B) [41][42][43]. The appearance of a hemoglobin-dominated principal component was expected.…”

Section: Raman Spectroscopic Signature Of Bloodmentioning

confidence: 99%

Discriminant Analysis of Raman Spectra for Body Fluid Identification for Forensic Purposes

Sikirzhytski

Virkler

Lednev

et al. 2010

AIP Conference Proceedings

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Detection and identification of blood, semen and saliva stains, the most common body fluids encountered at a crime scene, are very important aspects of forensic science today. This study targets the development of a nondestructive, confirmatory method for body fluid identification based on Raman spectroscopy coupled with advanced statistical analysis. Dry traces of blood, semen and saliva obtained from multiple donors were probed using a confocal Raman microscope with a 785-nm excitation wavelength under controlled laboratory conditions. Results demonstrated the capability of Raman spectroscopy to identify an unknown substance to be semen, blood or saliva with high confidence.

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Fourier transform Raman approach to structural correlation in hemoglobin derivatives

Cited by 34 publications

References 26 publications

Studies on heme release from normal and metal ion reconstituted hemoglobin mediated through ionic surfactant

Studies on heme release from normal and metal ion reconstituted hemoglobin mediated through ionic surfactant

Surface-Enhanced Raman Scattering of Whole Human Blood, Blood Plasma, and Red Blood Cells: Cellular Processes and Bioanalytical Sensing

Discriminant Analysis of Raman Spectra for Body Fluid Identification for Forensic Purposes

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