Adsorption of non-membrane proteins on the surface of model phospholipid membranes.
1. Two new methods are proposed for enhancement of the binding of hydrophilic proteins by liposomes. 2. An alkylating derivative of phosphatidic acid has been obtained by its reaction with N,N,N'-tris(2-chloroethyl)-N'-(p-formylphenyl)propylene-1,3-diamine. The alkylating activity of this derivative is very low due to the electron-acceptor effect of the formyl residue. Phosphatidylcholine liposomes which contain this alkylating derivative in the lipid bilayer may be obtained. The compound residing in the outer monolayer may be reduced by NaBH4. Upon reduction, the formyl residue is transformed into a hydroxymethyl residue. Therefore, the alkylating group of the compound is activated, and proteins may be attached covalently to the outer monolayer by alkylation with such chemically reactive liposomes. 3. Reaction of alkylating liposomes with myoglobin results in covalent binding of this hydrophilic protein. Complement-mediated leakage of such myoglobin-carrying liposomes may be induced by antibodies against myoglobin. 4. Modification of hydrophilic proteins with dansyl chloride results, even at small extents of modification, in a dramatic increase of the affinity of such proteins to phosphatidylcholine liposomes.
D000327:Adsorption; D000478:Alkylation; D000818:Animals; D003619:Dansyl Compounds; D007700:Kinetics; D008081:Liposomes; D009211:Myoglobin; D010712:Phosphatidic Acids; D011485:Protein Binding; D011506:Proteins; D012710:Serum Albumin, Bovine
D003619:Dansyl Compounds; D008081:Liposomes; D009211:Myoglobin; D010712:Phosphatidic Acids; D011506:Proteins; D012710:Serum Albumin, Bovine