title: Real-time analysis of porphyrin J-aggregation on a plant-esterase-functionalized surface using quartz crystal microbalance with dissipation monitoring.
abstract: The J-aggregation of meso-tetra (4-sulfonatophenyl) porphine (TPPS4) on a plant-esterase-functionalized surface in a 1:1 v/v mixture of 0.05 M HCl/ethanol (pH ∼1.38) was analyzed in real time using a quartz crystal microbalance with dissipation monitoring (QCM-D). Simultaneous changes in frequency (Δf) and energy dissipation (ΔD) correlated well with mass and structural changes during the sequential phases of slow nucleation, rapid aggregation, and equilibration in J-aggregation. The time-dependent mass adsorption could be quantitatively analyzed with a model, which integrated two simple equations obtained when the surface concentration of TPPS4 (Γ(TPPS4)) was below and above the critical aggregation surface concentration (CASC). This study provides a new view for the protein-induced J-aggregation process, which may be helpful for understanding the interactions of self-assembled nanostructures with biomolecules.
authors: State Key Laboratory of Heavy Oil Processing and Center for Bioengineering and Biotechnology, China University of Petroleum (East China) , Qingdao, Shandong 266555, P. R. China.
authors: Limin
authors: L
authors: Yang
authors: Lei
authors: L
authors: Jiang
authors: Weijing
authors: W
authors: Yao
authors: Junling
authors: J
authors: Liu
authors: Juan
authors: J
authors: Han
mesh_terms: D004950:Esterases / Q000737:chemistry*; D049329:Nanostructures / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D058525:Quartz Crystal Microbalance Techniques
chemical_list: D010940:Plant Proteins; D011506:Proteins; D004950:Esterases