Rearrangement of lipid ordered phases upon protein adsorption due to multiple site binding.
This study involves the interactions of proteins with Langmuir monolayers of a metal-chelating lipid, where adsorption is driven by a strong specific interaction between histidines on the proteins and divalent metal ions loaded into the lipid headgroups. A comparison of the structural rearrangement of the lipid film upon adsorption of myoglobin and a synthetic peptide, each of which have multiple histidines, with that upon the adsorption of lysozyme, which has only one histidine, suggests that the lipid rearrangement in the former case is due to the multiplicity of binding sites. The kinetics and manner of rearrangement change with the binding energy and film pressure.
Yim
H
H
Sandia National Laboratories, Albuquerque, New Mexico, USA.
Kent
M S
MS
Sasaki
D Y
DY
Polizzotti
B D
BD
Kiick
K L
KL
Majewski
J
J
Satija
S
S
D000327:Adsorption; D000818:Animals; D001665:Binding Sites; D002614:Chelating Agents / Q000737:chemistry; D002645:Chickens; D003300:Copper / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006736:Horses; D008055:Lipids / Q000737:chemistry*; D008567:Membranes, Artificial; D009113:Muramidase / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D009532:Nickel / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D044367:Phase Transition; D011485:Protein Binding
D002614:Chelating Agents; D008055:Lipids; D008567:Membranes, Artificial; D009211:Myoglobin; D010455:Peptides; D006639:Histidine; D003300:Copper; D009532:Nickel; D009113:Muramidase