A dramatic change in the interaction of Cu(II) with bio-peptides promoted by SDS--a model for complex formation on a membrane surface.
The extent of complex formation between Cu(II) and many biologically active oligopeptides has been shown to change significantly in the presence of SDS micelles, a recognized model for cell lipid membranes. Protonation constants of peptides can be increased by up to 2 log unit, especially when they contain hydrophobic side chains. Metal complex formation is generally less extensive and the conformations of peptides can be altered dramatically when compared to those in simple aqueous solution.
Bal
W
W
Institute of Chemistry, University of Wroclaw, Poland.
Kozlowski
H
H
Lisowski
M
M
Pettit
L
L
Robbins
R
R
Safavi
A
A
D000595:Amino Acid Sequence; D001127:Arginine Vasopressin / Q000737:chemistry / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D007987:Gonadotropin-Releasing Hormone / Q000737:chemistry / Q000378:metabolism; D008823:Micelles; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D013373:Substance P / Q000737:chemistry / Q000378:metabolism
D008823:Micelles; D009842:Oligopeptides; D001127:Arginine Vasopressin; D013373:Substance P; D007987:Gonadotropin-Releasing Hormone; D012967:Sodium Dodecyl Sulfate; D003300:Copper