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Fluorescence study of binding of adenosine derivatives to phospholipid membranes — effect of serum albumin

Authors
Journal
Journal of Molecular Structure
0022-2860
Publisher
Elsevier
Publication Date
Identifiers
DOI: 10.1016/s0022-2860(01)00500-2
Keywords
  • Liposomes
  • Serum Albumin
  • Adenosine Derivatives

Abstract

Abstract To increase stability against serum albumin and to minimize permeability increases caused by interaction with serum albumin, two types of liposomes consisting of various molar ratio lecithin/cholesterol were prepared. The adenosine derivatives were encapsulated in liposome vesicles of two sizes: 100 and 450 nm, prepared by modified reverse-phase evaporation method. The dependence of the stability of liposomes on the presence of serum albumin was studied by use of spectrofluorimetric technique. In the presence of serum albumin the studied ligands encapsulated into various types of liposome vesicles were released and this resulted in a decrease in the fluorescence spectrum of serum albumin in the region of tryptophan emission. Increase in the cholesterol content of the liposomes resulted in decreased leakage of the entrapped drugs, the effect of liposome size on leakage being less important.

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