Binding of bilirubin with albumin-coupled liposomes: implications in the treatment of jaundice

Biochim Biophys Acta. 2002 Aug 19;1564(1):219-26. doi: 10.1016/s0005-2736(02)00456-x.

Abstract

In the present study, we demonstrated the suitability of liposomes as a method of removing plasma bilirubin in hyperbilirubinemic rats. The liposomes have innate tendency to bind with bilirubin through hydrophobic interaction. Among different types of liposomes, the positively charged liposomes were found to have maximum affinity to free bilirubin. However, the entrapment or coupling of serum albumin on the surface of egg phosphatidylcholine liposomes can render a several-fold increase in their bilirubin binding capacity. The proteoliposomes were able to preferentially bind with bilirubin even in the presence of erythrocytes. Interestingly, these liposomes were found to displace bilirubin bound on the surface of erythrocytes as well. The results of the present study further demonstrate that albumin-bearing liposomes were equally effective in removing plasma bilirubin in experimental jaundiced animals. These observations indicate that liposome-mediated selective homing of excess plasma bilirubin to the liver cells (cf. hepatocytes) may help in the development of safer strategy for the treatment of hyperbilirubinemic conditions in the model animals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bilirubin / blood
  • Bilirubin / isolation & purification
  • Bilirubin / metabolism*
  • Cell Line
  • Disease Models, Animal
  • Erythrocytes / metabolism
  • Humans
  • In Vitro Techniques
  • Jaundice / blood*
  • Jaundice / therapy*
  • Liposomes
  • Male
  • Mononuclear Phagocyte System / metabolism
  • Rats
  • Rats, Wistar
  • Serum Albumin / metabolism*

Substances

  • Liposomes
  • Serum Albumin
  • Bilirubin