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Mechanistic insight into interaction of Sodium Dodecyl Sulphate to asialylated form of glycoprotein: A mimic of membrane protein-lipid system. | LitMetric

Mechanistic insight into interaction of Sodium Dodecyl Sulphate to asialylated form of glycoprotein: A mimic of membrane protein-lipid system.

Int J Biol Macromol

Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India. Electronic address:

Published: October 2017

AI Article Synopsis

  • The SDS-glycoprotein system simulates the interaction between membrane proteins and lipids, examining how the net charge of glycoproteins, which can fluctuate in acidic conditions, affects their behavior in pathological conditions like cancer and stroke.
  • Research on Asialofetuin (ASF) explores its interaction with SDS at different pH levels, revealing that at acidic pH (2, 3, 4), ASF aggregates due to electrostatic interactions with SDS, while at neutral pH (7.4), it becomes more structured and stable.
  • At lower pH levels, positively charged ASF forms amyloid structures, whereas at pH 7.4, a hydrophobic interaction leads to an increase in α

Article Abstract

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

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Source
http://dx.doi.org/10.1016/j.ijbiomac.2017.05.026DOI Listing

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