Related Experiment Video
Updated: Jan 2, 2026

Electronic Tongue Generating Continuous Recognition Patterns for Protein Analysis
Published on: September 16, 2014
Förster Resonance Energy Transfer-Mediated Globular Protein Sensing Using Polyelectrolyte Complex Nanoparticles
Hrishikesh Talukdar1, Sarathi Kundu1
1Soft Nano Laboratory, Physical Sciences Division, Institute of Advanced Study in Science and Technology, Vigyan Path, Paschim Boragaon, Garchuk, Guwahati 781035, Assam, India.
Abstract:
Polyelectrolyte complex nanoparticles (PEC NPs) are synthesized using two oppositely charged polyelectrolytes, i.e., anionic poly(sodium 4-styrene sulfonate) (PSS) and cationic poly(diallyldimethylammoniumchloride), at molar mixing ratios (n -/n +) of ≈0.4, 0.67, 0.75, and 1.5 by applying consecutive centrifugation to modify the optical property of PSS. However, for n -/n + ≈ 0.75, PEC NPs exhibit a larger blue shift and a specific emission peak occurs at ≈278 nm for the 225 nm excitation. The mechanism of such modification of PSS emission after complex formation is proposed. This specific emission by PEC NPs nearly matches with the optical absorption wavelength of globular proteins. The emission intensity of PEC NPs is therefore quenched in the presence of globular proteins (bovine serum albumin, human serum albumin, lysozyme, and hemoglobin) through resonance energy transfer between the donor (PEC NPs) and acceptor (globular proteins). The spectral overlap integral and the variation of the separation distance from 1.8 to 2.5 nm between the donor and acceptor confirm the resonance energy transfer. Sensing of proteins by the PEC NPs is possible within the detection limit of 5 nM and therefore such PEC NPs can be used as an efficient and promising protein sensing material.
Related Concept Videos
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

