Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/14733
Title: Influence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozyme
Authors: Witoonsaridsilp W.
Panyarachun B.
Sarisuta N.
Müller-Goymann C.C.
Keywords: Charged liposomes
Lipid binding
Lysozyme proteins
Secondary structure
Secondary structures
Amines
Conformations
Drug interactions
Enzymes
Liposomes
Proteins
Sodium chloride
Zeta potential
Phospholipids
chloride
cholesterol
lysozyme
phosphatidylcholine
sodium chloride
alpha helix
aqueous solution
article
bilayer membrane
circular dichroism
concentration response
controlled study
electricity
infrared spectroscopy
lipid composition
liposomal delivery
molecular dynamics
particle size
pH
phosphorus nuclear magnetic resonance
physical chemistry
priority journal
protein lipid interaction
protein secondary structure
surface charge
zeta potential
Animals
Buffers
Chickens
Cholesterol
Circular Dichroism
Lipid Bilayers
Liposomes
Magnetic Resonance Spectroscopy
Muramidase
Particle Size
Phosphatidylcholines
Protein Structure, Secondary
Solutions
Spectroscopy, Fourier Transform Infrared
Issue Date: 2010
Abstract: The conformation of peptide and protein drugs in various microenvironments and the interaction with drug carriers such as liposomes are of considerable interest. In this study the influence of microenvironments such as pH, salt concentration, and surface charge on the secondary structure of a model protein, lysozyme, either in solution or entrapped in liposomes with various molar ratios of phosphatidylcholine (PC):cholesterol (Chol) was investigated. It was found that entrapment efficiency was more pronounced in negatively charged liposomes than in non-charged liposomes, which was independent of Chol content and pH of hydration medium. The occurrence of aggregation, decrease in zeta potential, and alteration of 31P NMR chemical shift of negatively charged lysozyme liposomes compared to blank liposomes suggested that the electrostatic interaction plays a major role in protein-lipid binding. Addition of sodium chloride could impair the neutralizing ability of positively charged lysozyme on negatively charged membrane via chloride counterion binding. Neither lysozyme in various buffer solutions with sodium chloride nor that entrapped in liposomes showed any significant change in their secondary structures. However, significant decrease in α-helical content of lysozyme in non-charged liposomes at higher pH and salt concentrations was discovered. © 2009.
URI: https://www.scopus.com/inward/record.uri?eid=2-s2.0-70549107962&doi=10.1016%2fj.colsurfb.2009.09.027&partnerID=40&md5=945d8d4659304a0bbc9588db9facac45
http://ir.swu.ac.th/jspui/handle/123456789/14733
ISSN: 9277765
Appears in Collections:SCOPUS 1983-2021

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