The binding of DNA to water soluble carbodiimide modified proteins.
Bovine serum albumin and human serum transferrin modified by the water soluble carbodiimides N-ethyl-N'-(3-dimethyl propylamino) carbodiimide (CDI) or N-ethyl-N'-(3-trimethyl propylammonium) carbodiimide (Me+CDI) to yield N-acylurea proteins bind pBR322 DNA reversibly showing electrostatic and non-electrostatic components in the binding energies (delta G overall). It is proposed that initially an electrostatic interaction arises from ion pair formation between the DNA phosphates and the N-acylurea entities. This is consolidated, in single stranded regions, by a second event in which it is suggested that the base guanine interacts with elements of the N-acylurea moieties through hydrogen bonding or a glyoxal-type addition.
Ariatti
M
M
Department of Biochemistry, University of Durban-Westville, South Africa.
Hawtrey
A O
AO
D001665:Binding Sites; D002234:Carbodiimides; D004247:DNA / Q000378:metabolism*; D004563:Electrochemistry; D006147:Guanine / Q000378:metabolism; D066298:In Vitro Techniques; D008956:Models, Chemical; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012995:Solubility; D013816:Thermodynamics; D014168:Transferrin / Q000378:metabolism; D014867:Water
D002234:Carbodiimides; D011506:Proteins; D014168:Transferrin; D014867:Water; D012710:Serum Albumin, Bovine; D006147:Guanine; D004247:DNA