Characterizing the Binding of Angiotensin Converting Enzyme I Inhibitory Peptide to Human Hemoglobin: Influence of Electromagnetic Fields.

PAPER pubmed Protein and peptide letters 2020 In vitro study Effect: mixed Evidence: Very low

Read original paper → DOI: 10.2174/1871530320666200425203636 PMID: 32334494 Evidence Lab

Abstract

BACKGROUND: Drug-protein complexes is one of the crucial factors when analyzing the pharmacokinetics and pharmacodynamics of a drug because they can affect the excretion, distribution, metabolism and interaction with target tissues. OBJECTIVES: The aim of this study was to investigate the interaction of human hemoglobin (Hb) and angiotensin I converting enzyme inhibitory peptide (ACEIP) in the absence and presence of different- frequency electromagnetic fields (EMF). METHODS: Various spectroscopic methods like fluorescence spectroscopy, ultraviolet, circular dichroism and conductometry techniques were applied to investigate Hb-ACEIP interaction in the absence and presence of EMF. RESULT: The presented spectroscopic studies indicated that EMF changed the interaction between Hb and ACEIP. The a-helix content of Hb decreased upon binding to ACEIP and conductivity of the solution enhanced upon binding. Based on Stern-Volmer equations, it could be stated that the Hb-ACEIP affinity was higher in the presence of EMF. CONCLUSION: It can be concluded that for patients who use the drug to control blood pressure, a low-frequency electromagnetic field would have a positive effect on the uptake of the drug.

AI evidence extraction

At a glance

Study type

In vitro study

Effect direction

mixed

Population

—

Sample size

—

Exposure

Evidence strength

Very low

Confidence: 74% · Peer-reviewed: yes

Main findings

Spectroscopic measurements indicated that electromagnetic fields (EMF) changed the interaction between human hemoglobin and an ACE inhibitory peptide. The α-helix content of hemoglobin decreased upon binding to ACEIP and solution conductivity increased upon binding; Stern–Volmer analysis suggested higher Hb–ACEIP affinity in the presence of EMF.

Outcomes measured

Hemoglobin (Hb)–ACE inhibitory peptide (ACEIP) binding/interaction
Hb secondary structure (α-helix content)
Solution conductivity
Binding affinity (Stern–Volmer analysis)

Limitations

EMF frequencies are described as different-frequency/low-frequency but not specified.
In vitro spectroscopic study; clinical implications are not directly tested in patients.
No sample size or replication details provided in the abstract.
Exposure metrics (e.g., field strength, SAR, duration) are not reported in the abstract.

View raw extracted JSON

{
    "study_type": "in_vitro",
    "exposure": {
        "band": null,
        "source": null,
        "frequency_mhz": null,
        "sar_wkg": null,
        "duration": null
    },
    "population": null,
    "sample_size": null,
    "outcomes": [
        "Hemoglobin (Hb)–ACE inhibitory peptide (ACEIP) binding/interaction",
        "Hb secondary structure (α-helix content)",
        "Solution conductivity",
        "Binding affinity (Stern–Volmer analysis)"
    ],
    "main_findings": "Spectroscopic measurements indicated that electromagnetic fields (EMF) changed the interaction between human hemoglobin and an ACE inhibitory peptide. The α-helix content of hemoglobin decreased upon binding to ACEIP and solution conductivity increased upon binding; Stern–Volmer analysis suggested higher Hb–ACEIP affinity in the presence of EMF.",
    "effect_direction": "mixed",
    "limitations": [
        "EMF frequencies are described as different-frequency/low-frequency but not specified.",
        "In vitro spectroscopic study; clinical implications are not directly tested in patients.",
        "No sample size or replication details provided in the abstract.",
        "Exposure metrics (e.g., field strength, SAR, duration) are not reported in the abstract."
    ],
    "evidence_strength": "very_low",
    "confidence": 0.7399999999999999911182158029987476766109466552734375,
    "peer_reviewed_likely": "yes",
    "keywords": [
        "electromagnetic fields",
        "low-frequency EMF",
        "hemoglobin",
        "ACE inhibitory peptide",
        "drug-protein interaction",
        "fluorescence spectroscopy",
        "circular dichroism",
        "conductometry",
        "Stern–Volmer"
    ],
    "suggested_hubs": []
}

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

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