作者: Nida Zaidi , Rizwan Hasan Khan
DOI: 10.1016/J.IJBIOMAC.2017.05.026
关键词:
摘要: The SDS-glycoprotein system is mimic of membrane protein-lipid system. Fate glycoprotein, conformation and the interactive forces involved in milieu are expected to be decided by net charge on glycoprotein that may change during acidic environment a range pathological states, including cancer, stroke, ischemia. Asialofetuin (ASF; asialylated form glycoprotein) SDS interaction studied when bears varying (i.e. at different pH's) steady state time-resolved spectroscopic, calorimetric microscopic approaches. interacts differently with ASF protein cationic (at pH 2, 3 4) anionic states (pH 7.4). undergo aggregation 4 whereas have enhancement α-helical structure 7.4 sub-micellar concentrations SDS. At 4, positively charged electrostatically negatively head groups SDS, leaving its hydrophobic tail free interact other protein-SDS complex consequently lead amyloid formation. However, 7.4, hydrophobically an increase content occurs constrains Trp51 decreases movement Trp conformers.