title: Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes.
abstract: The interaction of rice glutelin (RG) with amylose was characterized by spectroscopic and molecular docking studies. The intrinsic fluorescence of RG increased upon the addition of amylose. The binding sites, binding constant and thermodynamic features indicated that binding process was spontaneous and the main driving force of the interaction was hydrophobic interaction. The surface hydrophobicity of RG decreased with increasing amount of amylose. Furthermore, synchronous fluorescence and circular dichroism (CD) spectra provided data concerning conformational and micro-environmental changes of RG. With the concentration of amylose increasing, the polarity around the tyrosine residues increased while the hydrophobicity decreased. Alteration of protein conformation was observed with increasing of α-helix and reducing of β-sheet. Finally, a visual representation of two binding sites located in the amorphous area of RG was presented by molecular modeling studies.
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang 330047, Jiangxi, China.
authors.forename: Xingfeng
authors.initials: X
authors.lastname: Xu
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang 330047, Jiangxi, China. Electronic address: liuwei@ncu.edu.cn.
authors.forename: Wei
authors.initials: W
authors.lastname: Liu
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang 330047, Jiangxi, China.
authors.forename: Junzhen
authors.initials: J
authors.lastname: Zhong
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang 330047, Jiangxi, China.
authors.forename: Liping
authors.initials: L
authors.lastname: Luo
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang 330047, Jiangxi, China. Electronic address: liuchengmei@aliyun.com.
authors.forename: Chengmei
authors.initials: C
authors.lastname: Liu
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang 330047, Jiangxi, China.
authors.forename: Shunjing
authors.initials: S
authors.lastname: Luo
authors.affiliation: Golden Agriculture Biotech Company Limited, No. 100 Xinzhou Road, Nanchang 330000, Jiangxi, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D000688:Amylose / Q000378:metabolism*; D000817:Anilino Naphthalenesulfonates / Q000737:chemistry; D028464:Cucurbita / Q000737:chemistry; D005916:Globulins / Q000737:chemistry; D005983:Glutens / Q000737:chemistry* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D062105:Molecular Docking Simulation; D008969:Molecular Sequence Data; D012275:Oryza / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012639:Seeds / Q000737:chemistry; D016415:Sequence Alignment; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
chemical_list: D000817:Anilino Naphthalenesulfonates; D005916:Globulins; C027132:1-anilino-8-naphthalenesulfonate; D005983:Glutens; D000688:Amylose
keywords: Amylose; Conformation; Hydrophobic interaction; Molecular modeling; Rice glutelin