Unfolding-induced in Haemoglobin by Exposure to Electromagnetic Fields: A FTIR Spectroscopy Study

Calabrò, Emanuele; Magazù, Salvatore

doi:10.13005/ojc/300104

Cited by 20 publications

(7 citation statements)

References 20 publications

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“…As expected for pure PEO fibers, FTIR bands appeared at 2882, 1466, and 1344 cm −1 , corresponding to stretching, scissoring, and wagging vibrations, respectively, of the CH 2 groups present in PEO [ 50,51 ] ( Figure A and Figure S2, Supporting Information). The bands at 1282 and 842 cm −1 correspond to CH 2 twisting and CH 2 rocking, respectively.…”

Section: Resultssupporting

confidence: 53%

Nonwoven Hemostatic Dressings Formed by Contact Drawing of Interposed Polyethylene Oxide (PEO)‐Fibrinogen and PEO‐Thrombin Microfibers

Verma

Yaghoobi

Kreplak

et al. 2022

Adv Materials Inter

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Textiles containing interposed layers of polyethylene oxide (PEO)‐fibrinogen and PEO‐thrombin fibers are explored as biomaterials for hemostasis. The PEO‐fibrinogen and PEO‐thrombin fibers are formed by contact drawing, an approach that uses an entangled polymer solution and a pin array to form fibers by extension of liquid bridges. The interposition of the PEO‐fibrinogen and PEO‐thrombin fibers results in polymerization of a fibrin hydrogel mesh once the textile is hydrated. This fibrin hydrogel mesh displays the expected bands and diffraction peaks by Fourier‐transform infrared spectromicroscopy and X‐ray diffraction, respectively. The functionality of the hemostatic textiles formed from the interposed PEO‐fibrinogen and PEO‐thrombin fibers is demonstrated by analyzing human blood hemolysis, complement activation, protein adsorption, and platelet and leukocyte adhesion, indicating compatibility with human blood (hemolysis ratio <5%), with minimal inflammatory response (levels of terminal complement complex equivalent to plasma). The cytocompatibility and potential for cell remodeling of the fibrin hydrogel mesh formed by this process is evaluated with human dermal fibroblasts and human keratinocytes and it is found that both cell types attach and grow on the fibrin mesh. Finally, a whole blood clotting time of less than 30 s suggests a potential use of this material in hemorrhage control.

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Section: Resultssupporting

confidence: 53%

Nonwoven Hemostatic Dressings Formed by Contact Drawing of Interposed Polyethylene Oxide (PEO)‐Fibrinogen and PEO‐Thrombin Microfibers

Verma

Yaghoobi

Kreplak

et al. 2022

Adv Materials Inter

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“…Consequently, the solution has a high content of unreacted silicate gel and surface adsorbed proteins 31 . The presence of the bands corresponding to amide I and amide II at around 1640 cm −1 and 1530 cm −1 , respectively, indicates the high content of proteins in the C-S-H samples modified with the proteins at C/S ratio of 1.5 62 , 63 .…”

Section: Resultsmentioning

confidence: 98%

Effect of Biomolecules on the Nanostructure and Nanomechanical Property of Calcium-Silicate-Hydrate

Kamali

Ghahremaninezhad

2018

Sci Rep

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Inspired by nature, this paper investigates the effect of biomolecules, such as amino acids and proteins, on the nanostructure and mechanical stiffness of calcium-silicate-hydrate (C-S-H). Amino acids with distinct functional groups, and proteins with different structures and compositions were used in the synthesis of the C-S-H nanocomposite. The atomic structure was examined using X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR). The morphology was investigated using scanning electron microscopy (SEM) and atomic force microscopy (AFM). AFM nanoindentation was used to evaluate the Young’s modulus of the modified C-S-H. Positively charged, H-bond forming and hydrophobic amino acids were shown to influence the atomic structure of C-S-H. The effect of negatively charged amino acid on atomic structure was more pronounced at higher C/S ratio. A noticeable increase in silicate polymerization of C-S-H modified with proteins at high C/S ratio was observed. The microscopic examination demonstrated a globular morphology for all samples except for C-S-H modified with hemoglobin, which showed a platelet morphology. The Young’s modulus of C-S-H with amino acids and proteins showed a general reduction compared to that of the control C-S-H.

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“…The quenching effect on the spectra of amide II region was stronger than the quenching effect on the spectra in the amide I region. [47] This difference indicates that the magnetic field has more damping influence on the out of phase combination of N-H, in-plane bending, and C-N stretching vibrations modes than on the in-phase combination of C=O stretching vibrations coupled to the C-N stretching.…”

Section: Discussionmentioning

confidence: 97%

Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin

Darwish¹

2017

EJB

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Human serum albumin and β-amyloid were exposed to extremely low frequency (ELF) magnetic field of 1.5 mT intensity and 50 Hz frequency. The effects of exposure were investigated in the mid-infrared region by means of Fourier selfdeconvolution spectroscopic analysis. The experimental results suggest that exposure to the ELF magnetic field has reversible effects on the out of phase combination of N-H in plane bending and C-N stretching vibrations of the secondary structures of the two proteins. The exposure of β-amyloid and human serum albumin to ELF magnetic field affected the absorption spectra of the vibration bands by changes in peak positions for the amide II bands and changes of intensities in most of the bands in the amide I and amide II regions. In the fingerprint region, the most sensitive vibrations to the magnetic field are found to be in the (720-600) cm-I range. After removing the magnetic field, it took the vibration bands more than 10 minutes of a gradual change toward returning to their original spectra, obtained before the exposure. It is suggested that hydrogen bonds can alter the frequency of a stretching vibration depending on the increase or decrease of strain on the vibrations.

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Unfolding-induced in Haemoglobin by Exposure to Electromagnetic Fields: A FTIR Spectroscopy Study

Cited by 20 publications

References 20 publications

Nonwoven Hemostatic Dressings Formed by Contact Drawing of Interposed Polyethylene Oxide (PEO)‐Fibrinogen and PEO‐Thrombin Microfibers

Nonwoven Hemostatic Dressings Formed by Contact Drawing of Interposed Polyethylene Oxide (PEO)‐Fibrinogen and PEO‐Thrombin Microfibers

Effect of Biomolecules on the Nanostructure and Nanomechanical Property of Calcium-Silicate-Hydrate

Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin

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