Molecular evidence of stereo-specific lactoferrin dimers in solution.
Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.
Persson
Björn A
BA
Department of Theoretical Chemistry, Lund University, Sweden. bjorn.persson@teokem.lu.se
Lund
Mikael
M
Forsman
Jan
J
Chatterton
Dereck E W
DE
Akesson
Torbjörn
T
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007781:Lactoferrin / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012996:Solutions; D013237:Stereoisomerism; D013379:Substrate Specificity
D012996:Solutions; D007781:Lactoferrin