Solid-film sampling method for the determination of protein secondary structure by Fourier transform infrared spectroscopy

Zhang, Junting; Zhang, Xiaoning; Zhang, Fan; Yu, Shaoning

doi:10.1007/s00216-017-0390-y

Cited by 17 publications

(16 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HSA proteins do not have a Albumin peaks at 1650 and 1657 cm −1 refer to 60.3% of the total area of the second derivative ( Figure 1b), and peak 1655 cm −1 of trypsin refer to 11.2%, which agrees with the data obtained from the DSSP, STRIDE, and the secondary structure assigned by authors of the X-ray structures PDB codes 1AO6 (HSA) and 1FMG porcine beta trypsin) [34][35][36][37][38][39] (Table 3). HSA proteins do not have a maximum at the second derivative deconvolution curves that correspond to a random coil conformation defined by the range of 1640-1649 cm −1 [33], which is also consistent with the previous FTIR studies [33,[40][41][42].…”

Section: Spectral Studies Of Native Protein Structuressupporting

confidence: 91%

“…In addition, the maxima of the second derivative (1628 cm −1 , 1638 cm −1 , and 1691 cm −1 ) characterize the β-sheet content, referring to the study of serum albumin [41]. The maxima of 1627 cm −1 and 1635 cm −1 of trypsin refer to 46.9% of the total area ( Figure 1d), which is consistent with the X-ray data ( Table 3) and was observed previously by FTIR [42].…”

Section: Spectral Studies Of Native Protein Structuresmentioning

confidence: 99%

See 1 more Smart Citation

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

et al. 2020

View full text Add to dashboard Cite

The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH4)2SO4). The changes in the secondary structure were studied at 23 °C and 80 °C by using the second derivative deconvolution method of the IR spectra. Our results demonstrated that the ability of the salts to stabilize/destabilize these two proteins correlates with the Hofmeister series of ions. At the same time, some exceptions were also observed. The destabilization of the native structures of both α-helical albumin and β-structural trypsin upon interaction with neutral salts leads to the formation of intermolecular β-sheets typical for amyloid fibrils or amorphous aggregates. Thus, our quantitative FTIR-spectroscopy analysis allowed us to further clarify the mechanisms and complexity of the neutral salt actions on protein structures which may lead to strategies preventing unwelcome misfolding of proteins.

show abstract

Section: Spectral Studies Of Native Protein Structuressupporting

confidence: 91%

Section: Spectral Studies Of Native Protein Structuresmentioning

confidence: 99%

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Acquisition of ATR-FTIR data of proteins in aqueous solution is not straightforward due to a number of experimental challenges. The first is that relatively high concentrations are needed to obtain spectra of reasonable quality 39 , 87 . This is due to the low affinity of protein for the ATR crystal surface, as the result of electrostatic repulsion between BSA and ZnSe and the weakly hydrophobic nature of the ZnSe surface 88 .…”

Section: Resultsmentioning

confidence: 99%

The molecular insights into protein adsorption on hematite surface disclosed by in-situ ATR-FTIR/2D-COS study

Barreto

Elzinga

Alleoni

2020

Sci Rep

View full text Add to dashboard Cite

Proteins are of ubiquitous interest in the Life Sciences but are of interest in the Geosciences as well because of the significant role these compounds play in the biogeochemical cycling of trace and nutrient elements. Structural changes resulting from the adsorption of proteins onto mineral surfaces may alter protein biological function and other environmental interactions. Iron oxides are major sinks of a range of environmental elements including organic compounds. In this study, the adsorption of the broadly studied model protein BSA onto the hematite mineral surface was characterized as a function of pH, ionic strength, and BSA concentration using in-situ Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) spectroscopy. BSA lost the α-helix and gain β-sheets in the secondary structure during adsorption on hematite. BSA adsorption was maximum at pH 5, a value close to the BSA isoelectric point (~ pH 5), and lower at pH 4 and pH 7. Increasing ionic strength decreased to total BSA adsorption. Two-dimensional correlation spectroscopy analysis of the ATR-FTIR spectra revealed that higher initial BSA concentration and the consequent higher BSA surface loading enhanced BSA adsorption by protein–protein interaction, which less ordered structures changes into more compact forms decrease, hence compacting the structural arrangement and could promoting multilayers/aggregation formation on the mineral surface. The activity of enzymes following adsorption on mineral surfaces requires further study.

show abstract

“…FTIR Spectroscopy: The conjugated protein samples were prepared for infrared measurements at 2 mg mL −1 using the solid-film sampling method. [36] FTIR spectra were recorded at 20 °C by a Bomen MB series FITR Spectrometer (Quebec, Canada) equipped with a dTGS detector and purged constantly with dry air. A 128-scan interferogram was collected in single-beam mode with 4 cm −1 resolution in each spectrum.…”

Section: Methodsmentioning

confidence: 99%

The Competitive Dynamic Binding of Some Blood Proteins Adsorbed on Gold Nanoparticles

Zhang

Shi

Zhang

et al. 2018

Part & Part Syst Charact

Self Cite

View full text Add to dashboard Cite

Nanoparticle (NP) surfaces are modified immediately by the adsorption of proteins when injected into human blood, leading to the formation of a protein corona. The protein‐coated NPs may be recognized by living cells. Furthermore, the adsorption of serum proteins is a continuous competitive dynamic process that is the key to exploring the bioapplication and biosafety of NPs. In this study, the competitive dynamic adsorption of some serum proteins on gold nanoparticles (AuNPs) is investigated by fluorescence emission, dynamic light scattering, and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. Serum proteins with different AuNPs binding affinities are used to address the competitive dynamic process of protein‐AuNP interactions in vitro. The results show that more abundant serum proteins, such as human serum albumin, adsorb on AuNPs first, and then the higher binding affinity and lower concentration serum proteins, such as fibrinogen (FIB), replace the abundant and lower binding affinity serum proteins. However, the lower binding affinity serum proteins, such as hemoglobin, do not replace the higher binding affinity proteins from the protein‐AuNP conjugates. During the dynamic exchange process, the larger the binding affinities difference between two proteins, the faster the exchange rate. This dynamic exchange process usually takes longer in inner protein‐AuNP conjugates (hard corona) than the external surface of protein‐AuNP conjugates (soft corona).

show abstract

Solid-film sampling method for the determination of protein secondary structure by Fourier transform infrared spectroscopy

Cited by 17 publications

References 31 publications

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

The molecular insights into protein adsorption on hematite surface disclosed by in-situ ATR-FTIR/2D-COS study

The Competitive Dynamic Binding of Some Blood Proteins Adsorbed on Gold Nanoparticles

Contact Info

Product

Resources

About