[Raman analysis of conformation changes of insulin solvent after being exposed to ELF pulsed electric field].
Abstract
Raman spectra of insulin solvents are presented before and after being exposed to the pulsed electric field with extremely low frequency 50 Hz (ELF). The covalences of the molecule were not affected and the changes of some secondary bonds such as hydrogen bonds and salt bonds were observed. Detailed analysis of these spectra indicates that the alpha-helix of insulin molecule was destroyed after the exposure, which is proved by the shift of the peak of the amide I region toward higher wave number and by the appearance of several new peaks: 1561 and 1594 cm(-1). The disulfides were affected by the weaken alpha-helix, and their vibrational modes were changed. Meanwhile the hydrogen bonding between the dimer are broken down which leads to the increase in the peak intensities at 1002 and at 1602 cm(-1).
AI evidence extraction
Main findings
Raman spectra before vs after exposure to a 50 Hz pulsed electric field showed no effect on covalent bonds but changes in secondary bonds (hydrogen and salt bonds). The analysis indicates destruction/weakening of insulin alpha-helix (amide I peak shift to higher wavenumber; new peaks at 1561 and 1594 cm(-1)), with associated changes in disulfide vibrational modes and breakdown of hydrogen bonding between dimers (increased peak intensities at 1002 and 1602 cm(-1)).
Outcomes measured
- Raman spectral changes in insulin solvent/molecule
- Protein secondary structure (alpha-helix) changes
- Hydrogen bond and salt bond changes
- Disulfide vibrational mode changes
- Dimer hydrogen bonding changes
Limitations
- No exposure duration reported
- No sample size or replication details reported in abstract
- No quantitative effect sizes or statistical analysis described in abstract
- In vitro/solvent Raman spectroscopy findings may not generalize to in vivo biological effects
Suggested hubs
-
el f-bioeffects
(0.86) Study examines biochemical/structural effects after exposure to an extremely low frequency (50 Hz) pulsed electric field.
View raw extracted JSON
{
"study_type": "in_vitro",
"exposure": {
"band": "ELF",
"source": "pulsed electric field",
"frequency_mhz": null,
"sar_wkg": null,
"duration": null
},
"population": null,
"sample_size": null,
"outcomes": [
"Raman spectral changes in insulin solvent/molecule",
"Protein secondary structure (alpha-helix) changes",
"Hydrogen bond and salt bond changes",
"Disulfide vibrational mode changes",
"Dimer hydrogen bonding changes"
],
"main_findings": "Raman spectra before vs after exposure to a 50 Hz pulsed electric field showed no effect on covalent bonds but changes in secondary bonds (hydrogen and salt bonds). The analysis indicates destruction/weakening of insulin alpha-helix (amide I peak shift to higher wavenumber; new peaks at 1561 and 1594 cm(-1)), with associated changes in disulfide vibrational modes and breakdown of hydrogen bonding between dimers (increased peak intensities at 1002 and 1602 cm(-1)).",
"effect_direction": "harm",
"limitations": [
"No exposure duration reported",
"No sample size or replication details reported in abstract",
"No quantitative effect sizes or statistical analysis described in abstract",
"In vitro/solvent Raman spectroscopy findings may not generalize to in vivo biological effects"
],
"evidence_strength": "very_low",
"confidence": 0.7399999999999999911182158029987476766109466552734375,
"peer_reviewed_likely": "yes",
"keywords": [
"Raman spectroscopy",
"insulin",
"pulsed electric field",
"extremely low frequency",
"50 Hz",
"protein conformation",
"alpha-helix",
"hydrogen bonds",
"disulfide bonds"
],
"suggested_hubs": [
{
"slug": "el f-bioeffects",
"weight": 0.85999999999999998667732370449812151491641998291015625,
"reason": "Study examines biochemical/structural effects after exposure to an extremely low frequency (50 Hz) pulsed electric field."
}
]
}
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