title: Biomolecular interaction study of Cyclolinopeptide A with human serum albumin.
abstract: The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C-37°C. The overall reaction was observed to be endothermic (ΔH = 204 kJ mol(-1)) and entropy driven (ΔS = 746 J mol(-1)K(-1)) with overall small changes to the tertiary structure.
authors: Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada S7N 5E5.
authors: Ben
authors: B
authors: Rempel
authors: Bo
authors: B
authors: Gui
authors: Jason
authors: J
authors: Maley
authors: Martin
authors: M
authors: Reaney
authors: Ramaswami
authors: R
authors: Sammynaiken
mesh_terms: D002942:Circular Dichroism; D004305:Dose-Response Relationship, Drug; D019597:Flax / Q000737:chemistry; D006801:Humans; D055767:Immobilized Proteins / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D020349:Surface Plasmon Resonance; D013816:Thermodynamics
chemical_list: D055767:Immobilized Proteins; D010456:Peptides, Cyclic; D012709:Serum Albumin; C055018:cyclolinopeptide A