A circular dichroism study of human erythrocyte ghost proteins during exposure to 2450 MHz microwave radiation.

Abstract

The effect of 2450 MHz microwave radiation on the proteins of human erythrocyte ghosts has been investigated using circular dichroism spectroscopy. A specially constructed waveguide inserted into the spectropolarimeter allowed the continuous recording of optical activity before, during and after microwave irradiation. The data indicate that high levels of microwave radiation (600 mW/g, specific absorption rate) induce decreases in alpha-helical conformation that may result from both thermal vibrations and increased strain on the intramolecular hydrogen bonds that maintain secondary structure. The latter effect may result from differential intramolecular interactions with the oscillating electric field. Spectrin (bands 1 and 2) isolated from the ghosts was more sensitive to microwave irradiation than intact ghosts, and spectrin-depleted vesicles were the least sensitive. The data, therefore, indicate that the alpha-helical conformation of spectrin is altered by high levels of microwave radiation.

AI evidence extraction

Main findings

Using circular dichroism spectroscopy, high-level 2450 MHz microwave irradiation (SAR 600 mW/g) was associated with decreases in alpha-helical conformation in erythrocyte ghost proteins. Isolated spectrin (bands 1 and 2) was reported to be more sensitive than intact ghosts, while spectrin-depleted vesicles were least sensitive, suggesting spectrin alpha-helical conformation is altered under these exposure conditions.

Outcomes measured

• Protein secondary structure (alpha-helical conformation) assessed by circular dichroism spectroscopy
• Relative sensitivity of spectrin vs intact ghosts vs spectrin-depleted vesicles to microwave irradiation

Limitations

• Exposure described as "high levels" (SAR 600 mW/g); generalizability to lower exposures not addressed in abstract
• In vitro preparation (erythrocyte ghosts/proteins) rather than whole-organism outcomes
• Duration of irradiation not reported in abstract
• Sample size and statistical details not reported in abstract

{
    "study_type": "in_vitro",
    "exposure": {
        "band": "microwave",
        "source": null,
        "frequency_mhz": 2450,
        "sar_wkg": 600,
        "duration": null
    },
    "population": "Human erythrocyte ghost proteins (including isolated spectrin)",
    "sample_size": null,
    "outcomes": [
        "Protein secondary structure (alpha-helical conformation) assessed by circular dichroism spectroscopy",
        "Relative sensitivity of spectrin vs intact ghosts vs spectrin-depleted vesicles to microwave irradiation"
    ],
    "main_findings": "Using circular dichroism spectroscopy, high-level 2450 MHz microwave irradiation (SAR 600 mW/g) was associated with decreases in alpha-helical conformation in erythrocyte ghost proteins. Isolated spectrin (bands 1 and 2) was reported to be more sensitive than intact ghosts, while spectrin-depleted vesicles were least sensitive, suggesting spectrin alpha-helical conformation is altered under these exposure conditions.",
    "effect_direction": "harm",
    "limitations": [
        "Exposure described as \"high levels\" (SAR 600 mW/g); generalizability to lower exposures not addressed in abstract",
        "In vitro preparation (erythrocyte ghosts/proteins) rather than whole-organism outcomes",
        "Duration of irradiation not reported in abstract",
        "Sample size and statistical details not reported in abstract"
    ],
    "evidence_strength": "low",
    "confidence": 0.7399999999999999911182158029987476766109466552734375,
    "peer_reviewed_likely": "yes",
    "keywords": [
        "2450 MHz",
        "microwave radiation",
        "circular dichroism",
        "erythrocyte ghosts",
        "spectrin",
        "alpha-helix",
        "protein conformation",
        "specific absorption rate"
    ],
    "suggested_hubs": []
}

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