Study of Thermal Dynamics of Defatted Bovine Serum Albumin in D2O Solution by Fourier Transform Infrared Spectra and Evolving Factor Analysis

Yuan, Bo; Murayama, Koichi; Yan, Huiming

doi:10.1366/000370207781745919

Cited by 18 publications

(17 citation statements)

References 52 publications

(66 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Here, the bands at 1613 cm À1 are assigned to heating-induced intermolecular b-sheet structures, while 1642 cm À1 reects random coils, 1662, 1670 and 1690 cm À1 are attributed to b-turns. 6,7 However, the assigning of the band at near 1632 cm À1 has been under controversy. Although it has been assigned to an intra-molecular b-sheet structure for many proteins, 27 several other studies suggest that it could be associated with the short segment chains connecting a-helix segments for some other proteins.…”

Section: Resultsmentioning

confidence: 99%

Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

Lü

Katzir

et al. 2015

Analyst

141

View full text Add to dashboard Cite

Attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy using a special waveguide based on a silver halide fiber was used for probing the heat-induced secondary structure and conformation changes of bovine serum albumin (BSA). From the secondary derivative and the curve fitting of the obtained ATR-FTIR spectra, the changes of the BSA secondary structure with temperature were clearly identified. Two different thermal denaturation temperature ranges (i.e., 50-52 and 80-82 °C, at which a change of the protein structure occurred) were determined, while only one denaturation temperature was previously identified via classical FTIR measurements. Additionally, taking advantage of two-dimensional correlation spectroscopy more detailed information on changes of the protein secondary structure was revealed. The developed method facilitates in situ, sensitive, and more in-depth probing of protein secondary structures, which represents a significant advancement compared to conventional characterization methods.

show abstract

Section: Resultsmentioning

confidence: 99%

Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

Lü

Katzir

et al. 2015

Analyst

141

View full text Add to dashboard Cite

show abstract

“…The molecular weight as well as the molar extinction coefficients used for the determination of albumin concentrations were: (1) 66.5 kDa; ε(278 nm) = 36850 M -1 cm -1 for fatted HSA and defatted HSA [46][47][48][49] (2) defatted BSA (66,430 Da; ε 280 = 44,300 M -1 cm -1 ); and (3) fatted PSA (67,900 Da; ε 280 = 45,600 M -1 cm -1 ) [22,36,48]. These values were obtained from the indicated references and product information documents from Sigma.…”

Section: Experimental Materials and Preparation Of Solutionsmentioning

confidence: 99%

Binding of Oxovanadium(IV) Complexes to Blood Serum Albumins

Cobbina

Mehtab²,

Correia³

et al. 2017

J. Mex. Chem. Soc.

View full text Add to dashboard Cite

In this work the binding of VIVO2+ and VIVO-complexes to serum albumins {human serum albumin (HSA), bovine serum albumin (BSA) and porcine serum albumin (PSA)} are studied using circular dichroism (CD), electron paramagnetic resonance (EPR) and visible absorption spectroscopy. The results confirm previous findings that VIVO2+ occupies at least two types of binding sites on albumin: ‘the strong vanadium binding site’ (designated by VBS1) and ‘the weak vanadium binding sites’ (designated by VBS2). VBS1 binds 1 mol equivalent of VIVO2+. On the other hand VBS2 correspond to binding of several mol equivalents of VIVO, and studies done with PSA in the presence of excess ZnII ions indicate that VSB2 corresponds to two distinct types of sites. The hyperfine coupling constant Az for VIVO2+ binding at VBS2 on HSA and BSA are all very similar (~168 × 10-4 cm-1) but differ slightly on PSA (~166 × 10-4 cm-1) due to differences in the binding sets. When (VIVO)-HSA systems are titrated with maltol ternary species of (maltol)m(VIVO)mHSA and (maltol)2m(VIVO)mHSA stoichiometry form which are clearly distinguishable from the binary (VIVO)-HSA system by the type and intensity of the CD spectra recorded. Changes are also observable in the intensity of the X-band EPR spectra, but not much in the hyperfine coupling constants Az, which are all in the range 166-167 × 10-4 cm-1. The results further demonstrate that the presence of maltol may enhance the binding of VIVO to albumin.

show abstract

“…IR and Raman probes are very often used in the study of proteins and peptides [1,3,9,10,13,40]. Vibrational spectra of proteins, especially in the Amide I and II regions, contain very rich information about the conformational secondary structure of various proteins.…”

Section: Protein Secondary Structuresmentioning

confidence: 99%

“…The temperature-dependent dynamics of individual secondary structures are modeled to follow the patterns similar to those observed in the actual experimental measurement [40] to make this study as realistic as possible. The real advantage of using the simulated data instead of the actual experimental protein IR spectra is that the assumed component spectra and their dynamics are a priori known without any ambiguity.…”

Section: Protein Secondary Structuresmentioning

confidence: 99%

Techniques of two-dimensional (2D) correlation spectroscopy useful in life science research

Noda

2015

Biomedical Spectroscopy and Imaging

View full text Add to dashboard Cite

Several illustrative examples are presented in this tutorial review to demonstrate the utility of 2D correlation spectroscopy, especially in life science applications. A set of IR spectra for a model protein system, which is undergoing complex thermally induced changes in the secondary structures, is analyzed by 2D correlation spectroscopy. The method of constructing 2D correlation maps from temperature-dependent IR spectra and their interpretation procedure are described. The resolution of overlapped protein IR bands by 2D correlation is demonstrated, and sequential order of spectral intensity changes is determined. Newly emerging techniques in the field, such as Pareto scaling, positive null-space projection, and 2D codistribution analysis, are discussed in some detail, in addition to the traditional application of 2D correlation spectroscopy.

show abstract

Study of Thermal Dynamics of Defatted Bovine Serum Albumin in D₂O Solution by Fourier Transform Infrared Spectra and Evolving Factor Analysis

Cited by 18 publications

References 52 publications

Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

Binding of Oxovanadium(IV) Complexes to Blood Serum Albumins

Techniques of two-dimensional (2D) correlation spectroscopy useful in life science research

Contact Info

Product

Resources

About