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A Phospholipase-A Activity in Soluble Leishmania Antigens Causes Instability of Liposomes Publisher Pubmed



Chavoshian O1, 2 ; Arabsalmani M1, 3 ; Jaafari MR1, 3, 4 ; Khamesipour A5 ; Abbasi A1 ; Saberi Z1 ; Badiee A1, 3
Authors
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Authors Affiliations
  1. 1. Nanotechnology Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran
  2. 2. School of Pharmacy, Zabol University of Medical Sciences, Zabol, Iran
  3. 3. Department of Pharmaceutical Nanotechnology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
  4. 4. Biotechnology Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran
  5. 5. Center for Research and Training in Skin Diseases and Leprosy, Tehran University of Medical Sciences, Tehran, Iran

Source: Current Drug Delivery Published:2020


Abstract

Aim: This study aimed to investigate the existence of phospholipase-A (PLA) activity in Soluble L. major Antigens (SLA) because of no reports for it so far. Liposomes were used as sensors to evaluate PLA activity. Objectives: Liposomal SLA consisting of Egg Phosphatidylcholine (EPC) or Sphingomyelin (SM) were prepared by two different methods in different pH or temperatures and characterized by Dynamic Light Scattering (DLS) and Thin Layer Chromatography (TLC). Methods: Lipid hydrolysis led to the disruption of EPC liposomal SLA in both methods but the Film Method (FM) produced more stable liposomes than the Detergent Removal Method (DRM). Result: The preparation of EPC liposomal SLA at pH 6 via FM protected liposomes from hydrolysis to some extent for a short time. EPC liposomes but not SM liposomes were disrupted in the presence of SLA. Conclusion: Therefore, a phospholipid without ester bond such as SM should be utilized in liposome formulations containing PLA as an encapsulating protein. © 2020 Bentham Science Publishers.
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