Interactions between DMPC liposomes and the serum blood proteins HSA and IgG.
The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements. HSA and IgG interact with liposomes forming molecular aggregates that remain stable at protein concentrations beyond those of total liposome coverage. Both HSA and IgG penetrate into the liposome bilayer. An ELISA assay indicates that the Fc region of IgG is the one that is immersed in the DMPC membrane. The liposome-protein interaction is mainly of electrostatic nature, but an important hydrophobic contribution is also present.
Sabín
Juan
J
Grupo de Biofísica e Interfases, Departamento de Física Aplicada, Facultad de Física, Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
Prieto
Gerardo
G
Ruso
Juan M
JM
Messina
Paula V
PV
Salgado
Francisco J
FJ
Nogueira
Montserrat
M
Costas
Miguel
M
Sarmiento
Félix
F
D002152:Calorimetry, Differential Scanning; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D024202:Electrophoretic Mobility Shift Assay; D004797:Enzyme-Linked Immunosorbent Assay; D005434:Flow Cytometry; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry*; D008027:Light; D008081:Liposomes / Q000737:chemistry*; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000737:chemistry*; D013500:Surface Tension; D013696:Temperature
D007074:Immunoglobulin G; D008081:Liposomes; D012709:Serum Albumin; D004134:Dimyristoylphosphatidylcholine