Medical/biological study (experimental study)

Microwave radiation can alter protein conformation without bulk heating med./bio.

By: de Pomerai DI, Smith B, Dawe A, North K, Smith T, Archer DB, Duce IR, Jones D, Candido EP

Published in: FEBS Lett 2003; 543 (1-3): 93-97

To study whether prolonged microwave exposure can directly affect protein conformation in vitro (because protein conformational changes are associated with a group of human diseases, the amyloidpathies), and whether this might underlie the observed induction of heat shock protein expression.

Exposure	Parameters
Exposure 1: 1 GHz Exposure duration: continuous for 3-48 h	power: 0.5 W SAR: 20 mW/kg (15-20 mW/kg)

Exposure source	TEM cell waveguide
Setup	exposed plates placed centrally on the waveguide of the TEM cell
Sham exposure	A sham exposure was conducted.

Measurand	Value	Type	Method	Mass	Remarks
power	0.5 W	-	-	-	-
SAR	20 mW/kg	-	calculated	-	15-20 mW/kg

Daniells C et al. (1998): Transgenic nematodes as biomonitors of microwave-induced stress

Exposed system:

isolated bio./chem. substance
bovine serum albumin (BSA) solution; bovine insulin solution
invertebrate
Caenorhabditis elegans/PC161 (nematode; growing on HT115 bacteria carrying either the yk663f6-derived RNA interference construct (full-length heat-shock transcription factor (HSF) cDNA) or the L4440 feeding vector only)
whole body

Investigated system:

Time of investigation:

Microwave exposure enhances the aggregation of bovine serum albumin in a time- and temperature-dependent manner. Microwave irradiation also promotes amyloid fibril formation by bovine insulin at 60°C. These changes in protein conformation are not accompanied by measurable temperature changes. Limited denaturation of cellular proteins could explain previous observation (publication 4466) that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. It is also shown that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock transcription factor function.

Study character:

Fasseas MK et al. (2015): Response of Caenorhabditis elegans to wireless devices radiation exposure
Beyer C et al. (2014): Real-time assessment of possible electromagnetic-field-induced changes in protein conformation and thermal stability
Sefidbakht Y et al. (2013): Effects of 940 MHz EMF on Luciferase solution: structure, function, and dielectric studies
Damm M et al. (2012): Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols
Belyaev IY et al. (2009): Microwaves from UMTS/GSM mobile phones induce long-lasting inhibition of 53BP1/gamma-H2AX DNA repair foci in human lymphocytes
Mousavy SJ et al. (2009): Effects of mobile phone radiofrequency on the structure and function of the normal human hemoglobin
Mohammadzadeh M et al. (2009): Electromagnetic field (EMF) effects on channel activity of nanopore OmpF protein
George DF et al. (2008): Non-Thermal effects in the microwave induced unfolding of proteins observed by chaperone binding