title: Inhibitory effects of β-ionone on amyloid fibril formation of β-lactoglobulin.
abstract: β-Lactoglobulin (β-LG) is the major constituent of whey food, which has been shown to interact with a wide range of aroma compounds. In the present work, a model aroma compound, β-ionone, is used to investigate the influence of aroma compounds on the urea-induced unfolding of β-LG at pH 7.0. β-Ionone is observed to enhance the stability of β-LG at pH 7.0. Moreover, the amyloid fibrils are observed when β-LG at pH 7.0 is incubated for 12-20 days at 37 °C in the presence of 3-5M urea. However, the formation of amyloid fibrils is inhibited when β-ionone is added into the samples and the inhibitory effects follow a concentration-dependent fashion. There is a clear correlation between Cm and lag time. The correlation demonstrates that protein stability affects the amyloid fibril formation of β-LG. The results highlight the critical role of protein stability and provide an approach to prevent the formation of amyloid fibrils in vitro.
authors: Department of Physics, Science of College, Nanjing Agricultural University, Nanjing 210095, PR China.
authors: Baoliang
authors: B
authors: Ma
authors: Department of Applied Mathematics, Science of College, Nanjing Agricultural University, Nanjing 210095, PR China. Electronic address: youx@njau.edu.cn.
authors: Xiong
authors: X
authors: You
authors: Department of Physics, Science of College, Nanjing Agricultural University, Nanjing 210095, PR China.
authors: Fujiao
authors: F
authors: Lu
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry* / Q000648:ultrastructure; D008958:Models, Molecular; D015394:Molecular Structure; D045792:Norisoprenoids / Q000737:chemistry / Q000494:pharmacology*; D011487:Protein Conformation; D058767:Protein Unfolding / Q000187:drug effects; D014508:Urea / Q000494:pharmacology
chemical_list: D000682:Amyloid; D007782:Lactoglobulins; D045792:Norisoprenoids; D014508:Urea; C008157:beta-ionone
keywords: Amyloid fibrils; Lag time; Protein stability; β-Ionone; β-Lactoglobulin