Publication:
Influence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozyme

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Issued Date

2010

Resource Type

Article

File Type

application/pdf

ISSN

9277765

DOI

10.1016/j.colsurfb.2009.09.027

Other identifier(s)

2-s2.0-70549107962

Rights Holder(s)

Scopus

Bibliographic Citation

Colloids and Surfaces B: Biointerfaces. Vol 75, No.2 (2010), p.501-509

Suggested Citation

Witoonsaridsilp W., Panyarachun B., Sarisuta N., Müller-Goymann C.C. Influence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozyme. Colloids and Surfaces B: Biointerfaces. Vol 75, No.2 (2010), p.501-509. doi:10.1016/j.colsurfb.2009.09.027 Retrieved from: https://hdl.handle.net/20.500.14740/7628

Title

Influence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozyme

Author(s)

Witoonsaridsilp W.
 Panyarachun B.
 Sarisuta N.
 Müller-Goymann C.C.

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.

Subject(s)

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

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URI

https://hdl.handle.net/20.500.14740/7628

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Scopus: Year 1983-2021

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