Microwave radiation can alter protein conformation without bulk heating

• Published in: FEBS letters 2003-05, Vol.543 (1), p.93-97
• Main Authors: de Pomerai, David I., Smith, Brette, Dawe, Adam, North, Kate, Smith, Tim, Archer, David B., Duce, Ian R., Jones, Donald, Candido, E.Peter M.
• Format: Article
• Language: English
• Subjects: Amyloid - radiation effects; Amyloid - ultrastructure; Amyloid fibril; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Heat-Shock Proteins - pharmacology; Hot Temperature; Insulin - radiation effects; Microwave radiation; Microwaves; Non-thermal; Protein aggregation; Protein Conformation - drug effects; Protein Conformation - radiation effects; RNA Interference; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - radiation effects; Transcription Factors - antagonists & inhibitors; Transcription Factors - genetics
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(03)00413-7

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°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.