title: Thermal aggregation of glycated bovine serum albumin.
abstract: Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes. In this work, we firstly reported a study on the glycation and oxidation effects on the structure of bovine serum albumin (BSA). The experimental approach is based on the study of conformational changes of BSA at secondary and tertiary structures by FTIR absorption and fluorescence spectroscopy, respectively. Secondly, we analysed the thermal aggregation process on BSA glycated with different glucose concentrations. Additional information on the aggregation kinetics are obtained by light scattering measurements. The results show that glycation process affects the native structure of BSA. Then, the partial unfolding of the tertiary structure which accompanies the aggregation process is similar both in native and glycated BSA. In particular, the formation of aggregates is progressively inhibited with growing concentration of glucose incubated with BSA. These results bring new insights on how aggregation process is affected by modification of BSA induced by glycation.
authors.affiliation: Université de La Réunion, Laboratoire de Biochimie et Génétique Moléculaire (LBGM)-Groupe d'Etude sur l'Inflammation Chronique et l'Obésité (GEICO), Saint Denis de La Réunion, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: Rondeau
authors.forename: Giovanna
authors.initials: G
authors.lastname: Navarra
authors.forename: Francesco
authors.initials: F
authors.lastname: Cacciabaudo
authors.forename: Maurizio
authors.initials: M
authors.lastname: Leone
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Bourdon
authors.forename: Valeria
authors.initials: V
authors.lastname: Militello
mesh_terms: D000818:Animals; D002417:Cattle; D005947:Glucose / Q000737:chemistry; D017127:Glycation End Products, Advanced / Q000737:chemistry; D006031:Glycosylation; D006358:Hot Temperature; D066298:In Vitro Techniques; D007700:Kinetics; D010084:Oxidation-Reduction; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D017550:Spectroscopy, Fourier Transform Infrared; D014364:Tryptophan / Q000737:chemistry; D056811:Unfolded Protein Response; D000093423:Glycated Serum Albumin
chemical_list: D017127:Glycation End Products, Advanced; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D014364:Tryptophan; D005947:Glucose; D000093423:Glycated Serum Albumin