Controlled Assembly of Protein in Glass Capillary
Citations Over TimeTop 13% of 2010 papers
Abstract
By means of a slow drying process and the control of surface charge characteristics, protein stripe patterns were readily prepared on the luminal surface of a capillary. We systematically studied the effects of surface properties, pH, and protein concentration on pattern formation using optical microscopy, atomic force microscopy, and quartz crystal microbalance measurement. By balancing these parameters, a broad selection of proteins could be assembled within a capillary with well-defined stripe patterns. Neutravidin, one of the model proteins, was specifically chosen to demonstrate the bioactivity retained through the assembly process by interaction with fluorescently labeled biotin motifs. This technique therefore offers a facile approach for patterning proteins and other biomacromolecules in capillary tubes.
Related Papers
- → Label-Free, Real-Time Interaction and Adsorption Analysis 2: Quartz Crystal Microbalance(2013)16 cited
- → A Study on Regenerative Quartz Crystal Microbalance(2022)7 cited
- → ASSESMENT OF FOULING POTENTIAL OF BIOPOLYMERS ISOLATED FROM SURFACE WATER USING QUARTZ CRYSTAL MICROBALANCE WITH DISSIPATION MONITORING（QCM-D）(2021)3 cited
- → Quartz Crystal Microbalance (QCM): An Alternative Analytical Method for Investigation in Real-Time of Liquid Properties(2010)2 cited
- → Electrospun biotin- and streptavidin-coated quartz crystal microbalance surfaces: characterization and mass sensing performance using OpenQCM(2023)