Fluorescent turn-on sensing of albumin proteins (BSA and ovalbumin) using vitamin B6 cofactor derived Schiff base
•Vitamin B6 cofactor derived Schiff base L was applied for the fluorescence turn-on detection of BSA and OVA.•The weakly emissive L showed a significant fluorescence enhancement in the presence of OVA and BSA.•The receptor L showed micromolar detection limit for BSA and OVA.•Molecular docking and dy...
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Published in: | Methods (San Diego, Calif.) Vol. 206; pp. 69 - 76 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
Elsevier Inc
01-10-2022
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Subjects: | |
Online Access: | Get full text |
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Summary: | •Vitamin B6 cofactor derived Schiff base L was applied for the fluorescence turn-on detection of BSA and OVA.•The weakly emissive L showed a significant fluorescence enhancement in the presence of OVA and BSA.•The receptor L showed micromolar detection limit for BSA and OVA.•Molecular docking and dynamics simulation studies were performed to examine the BSA/OVA-L complex formation.•Practical utility of L was validated by quantifying BSA and OVA in various real biological samples.
The detection of albumin proteins with high accuracy by facile analytical approaches is important for the diagnosis of various diseases. This manuscript introduced an easy-to-prepare Schiff base L by condensing vitamin B6 cofactor pyridoxal 5'-phosphate (PLP) with 2-aminothiophenol for the fluorescence turn-on sensing of bovine serum albumin (BSA) and ovalbumin (OVA). The weakly emissive L showed a significant fluorescence enhancement at 485 and 490 nm in the presence of OVA and BSA with an estimated sensitivity limit of 1.7 µM and 0.3 µM, respectively. The formation of protein-ligand complex restricted the free intramolecular rotation of L is expected to show the selective fluorescence enhancement. The molecular docking and molecular dynamics simulations were performed to examine the binding affinity and modes between BSA/OVA and L. The practical utility of L as a fluorescent turn-on sensor was validated by quantifying BSA and OVA in various real biological samples of milk, serum, egg white and urine with good recovery percentages. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1046-2023 1095-9130 |
DOI: | 10.1016/j.ymeth.2022.08.014 |