Trifluoroethanol increases albumin's susceptibility to chemical modification.
Acrolein-dependent chemical modification is implicated in the etiology of postoperative cognitive dysfunction (POCD). We examined this process further using human serum albumin (HSA), which is a target of acrolein modification and contains anesthetic binding sites. We tested whether trifluoroethanol (TFE), which mimics inhaled anesthetics, affects the susceptibility of HSA to modification by acrolein. We observed that acrolein promoted the formation of fluorescent adducts. TFE (10%) increased the amount of acrolein-HSA adducts. TFE (40%) caused a 5-fold increase in adduct formation. Acrolein also increased tryptophan anisotropy of HSA, which was further increased by TFE (10%). Acrolein-induced protein cross-linking was also increased in the presence of TFE (40%). These observations suggest that TFE promotes acrolein-induced modification of HSA, supporting a putative mechanism for POCD.
Craig
Heather D
HD
Department of Biochemistry, Kansas City University of Medicine and Biosciences, 1750 Independence Avenue, Kansas City, MO 64106, USA.
Eklund
Joshua D
JD
Seidler
Norbert W
NW
D000171:Acrolein / Q000031:analogs & derivatives / Q000378:metabolism / Q000633:toxicity; D018685:Anesthetics, Inhalation / Q000737:chemistry / Q000378:metabolism / Q000633:toxicity; D001665:Binding Sites; D055592:Biophysical Phenomena; D003072:Cognition Disorders / Q000209:etiology / Q000378:metabolism; D005453:Fluorescence; D006801:Humans; D066298:In Vitro Techniques; D008954:Models, Biological; D011183:Postoperative Complications / Q000209:etiology / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D012709:Serum Albumin / Q000737:chemistry* / Q000187:drug effects* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D014270:Trifluoroethanol / Q000633:toxicity*; D014364:Tryptophan / Q000737:chemistry
D018685:Anesthetics, Inhalation; D012709:Serum Albumin; D014270:Trifluoroethanol; D000171:Acrolein; D014364:Tryptophan