Imaging macromolecular interactions at an interface.
Important physiological, pathological, and technological processes occur at continuous and dispersed phase interfaces. Understanding these processes is limited by inability to quantitate molecular events occurring at the interface. To provide a model-independent measurement of protein concentration and mobility at the interface, we employed confocal laser scanning microscopy (CLSM). Fluorescently labeled albumin and fibrinogen were studied singly, pairwise, and with a surfactant, Pluronic F-127, in aqueous droplets. CLSM enables measurement of molecular behaviors manifest as surface inhomogeneity and of biophysical quantities including partitioning between the bulk and the gas-liquid (GL) interface. We conclude that albumin and fibrinogen behave substantially differently at the GL interface, adsorption from multispecies solutions is fundamentally different than adsorption from solutions of single species, and surfactants can inhibit proteins from occupying the interface.
Lampe
Joshua W
JW
Center for Resuscitation Science, Department of Emergency Medicine, Hospital of the University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Liao
Zhengzheng
Z
Dmochowski
Ivan J
IJ
Ayyaswamy
Portonovo S
PS
Eckmann
David M
DM
D000418:Albumins / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry*; D046911:Macromolecular Substances / Q000737:chemistry*; D018613:Microscopy, Confocal; D010316:Particle Size; D020442:Poloxamer / Q000737:chemistry; D012996:Solutions; D013499:Surface Properties
D000418:Albumins; D046911:Macromolecular Substances; D012996:Solutions; D020442:Poloxamer; D005340:Fibrinogen