Microwave radiation can alter protein conformation without bulk heating.
Exposure to microwave radiation enhances the aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner. Microwave radiation also promotes amyloid fibril formation by bovine insulin at 60 degrees C. These alterations in protein conformation are not accompanied by measurable temperature changes, consistent with estimates from field modelling of the specific absorbed radiation (15-20 mW kg(-1)). Limited denaturation of cellular proteins could explain our previous observation that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. We also show that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock factor function.
de Pomerai
David I
DI
School of Life and Environmental Sciences, University of Nottingham, University Park, NG7 2RD, Nottingham, UK. david.depomerai@nottingham.ac.uk
Smith
Brette
B
Dawe
Adam
A
North
Kate
K
Smith
Tim
T
Archer
David B
DB
Duce
Ian R
IR
Jones
Donald
D
Candido
E Peter M
EP
D000682:Amyloid / Q000528:radiation effects / Q000648:ultrastructure; D029742:Caenorhabditis elegans Proteins; D006360:Heat-Shock Proteins / Q000494:pharmacology; D006358:Hot Temperature; D007328:Insulin / Q000528:radiation effects; D008872:Microwaves; D011487:Protein Conformation / Q000187:drug effects / Q000528:radiation effects*; D034622:RNA Interference; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000528:radiation effects; D014157:Transcription Factors / Q000037:antagonists & inhibitors / Q000235:genetics
D000682:Amyloid; D029742:Caenorhabditis elegans Proteins; D006360:Heat-Shock Proteins; D007328:Insulin; D014157:Transcription Factors; C108431:hsp-16.2 protein, C elegans; D012710:Serum Albumin, Bovine