A protein structure-dependent fluorescent probe for real-time β-lactoglobulin detection

Area of Science:

• Biochemistry
• Analytical Chemistry
• Molecular Biology

Background:

• Real-time detection of beta-lactoglobulin (a key milk protein) is crucial for rapid beverage quality control.
• Conventional methods for protein analysis are often time-consuming and require specialized laboratory equipment, hindering on-site applications.

Purpose of the Study:

• To develop a novel, structure-dependent fluorescent probe (DNP) for the selective and sensitive detection of beta-lactoglobulin.
• To enable real-time, on-site analysis of beta-lactoglobulin in complex matrices like beverages.

Main Methods:

• Design of a protein structure-dependent fluorescent probe (DNP) targeting the central calyx binding site of beta-lactoglobulin.
• Utilizing direct non-covalent interactions for fluorescence "turn-on" detection without enzymatic reactions.
• Application of DNP for visualization in living cells and fluorescence-based quantitative analysis in beverage samples, considering matrix effects.

Main Results:

• DNP exhibited high selectivity and sensitivity for beta-lactoglobulin detection via a fluorescence "turn-on" mechanism.
• Successful visualization of exogenous beta-lactoglobulin within living cells.
• Demonstrated feasibility for real-time preliminary and quantitative assessment of beta-lactoglobulin in beverage samples, even with matrix interference.

Conclusions:

• DNP is a promising tool for rapid, structure-specific detection of beta-lactoglobulin.
• The probe facilitates immediate on-site beverage quality analysis, overcoming limitations of conventional methods.
• DNP holds potential for advancing real-time analytical workflows in food and beverage industries.