New insights into bioprotective effectiveness of disaccharides: an FTIR study of human haemoglobin aqueous solutions exposed to static magnetic fields.

Journal of biological physics · 2012 · Mixed · Low evidence

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MixedLow evidencePaper 3189

Study snapshot

PublicationJournal of biological physics · 2012

Study typein_vitro

Reported directionMixed

Evidence ratingLow

Abstract

The aim of this study was the investigation of static magnetic field effects on haemoglobin secondary structure and the bioprotective effectiveness of two disaccharides, sucrose and trehalose. Samples of haemoglobin aqueous solutions, in the absence and in the presence of sucrose and trehalose, were exposed to a uniform magnetic field at 200 mT, which is the exposure limit established by the ICNIRP recommendation for occupational exposure. Spectral analysis by FTIR spectroscopy after 3 and 7 h of exposure revealed a decrease in the amide A vibration band for haemoglobin in bi-distilled water solution. Analogue exposures did not produce any appreciable change of amide A for haemoglobin in sucrose and trehalose solutions. Otherwise, no relative increase of [Formula: see text]-sheet contents in amide I and II regions was detected for haemoglobin aqueous solutions, leading us to exclude the hypothesis that static magnetic fields can induce the formation of aggregates in the protein. In addition, a decrease in CH(3) stretching linkages occurred for haemoglobin in bi-distilled water solution after exposure, which was not observed for haemoglobin in sucrose and trehalose aqueous solutions, providing further evidence of a bioprotective compensatory mechanism of such disaccharides.

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AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typein_vitro

Effect directionmixed

PopulationNot supplied

Sample sizeNot supplied

Exposurestatic · 3 and 7 h

Evidence strengthLowConfidence: 78% · Peer reviewed: yes

Main findings

Human haemoglobin aqueous solutions exposed to a uniform 200 mT static magnetic field showed a decrease in the amide A vibration band and a decrease in CH(3) stretching linkages when haemoglobin was in bi-distilled water. Comparable exposures produced no appreciable change in amide A and did not show the CH(3) change when haemoglobin was in sucrose or trehalose solutions. No increase in β-sheet contents in amide I and II regions was detected, and the authors excluded the hypothesis that static magnetic fields induce protein aggregation under these conditions.

Outcomes measured

Haemoglobin secondary structure (FTIR; amide A band)
Amide I and II regions (β-sheet content/aggregation hypothesis)
CH(3) stretching linkages

Limitations

In vitro study in haemoglobin aqueous solutions; no human health outcomes reported
Sample size not reported in abstract
Only one field strength (200 mT) and limited exposure durations (3 and 7 h) reported
Outcomes are spectroscopic/protein-structure markers; generalizability to in vivo conditions unclear

View raw extracted JSON

{
  "study_type": "in_vitro",
  "exposure": {
    "band": "static",
    "source": "occupational",
    "frequency_mhz": null,
    "sar_wkg": null,
    "duration": "3 and 7 h"
  },
  "population": null,
  "sample_size": null,
  "outcomes": [
    "Haemoglobin secondary structure (FTIR; amide A band)",
    "Amide I and II regions (β-sheet content/aggregation hypothesis)",
    "CH(3) stretching linkages"
  ],
  "main_findings": "Human haemoglobin aqueous solutions exposed to a uniform 200 mT static magnetic field showed a decrease in the amide A vibration band and a decrease in CH(3) stretching linkages when haemoglobin was in bi-distilled water. Comparable exposures produced no appreciable change in amide A and did not show the CH(3) change when haemoglobin was in sucrose or trehalose solutions. No increase in β-sheet contents in amide I and II regions was detected, and the authors excluded the hypothesis that static magnetic fields induce protein aggregation under these conditions.",
  "effect_direction": "mixed",
  "limitations": [
    "In vitro study in haemoglobin aqueous solutions; no human health outcomes reported",
    "Sample size not reported in abstract",
    "Only one field strength (200 mT) and limited exposure durations (3 and 7 h) reported",
    "Outcomes are spectroscopic/protein-structure markers; generalizability to in vivo conditions unclear"
  ],
  "evidence_strength": "low",
  "confidence": 0.78,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "static magnetic field",
    "200 mT",
    "ICNIRP occupational limit",
    "haemoglobin",
    "FTIR spectroscopy",
    "sucrose",
    "trehalose",
    "protein secondary structure",
    "amide A",
    "amide I",
    "amide II"
  ],
  "suggested_hubs": [
    {
      "slug": "occupational-exposure",
      "weight": 0.6,
      "reason": "Exposure level described as ICNIRP occupational exposure limit (200 mT) for static magnetic fields."
    },
    {
      "slug": "who-icnirp",
      "weight": 0.45,
      "reason": "ICNIRP recommendation is explicitly referenced as the exposure limit."
    }
  ]
}

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AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1007/s10867-010-9209-1
PubMed: 23277670

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