Chemical Capture and Sensing of Bovine Serum Albumin with Phenothiazinylcarbaldehyde-Labeled 2′-Deoxyuridine

Abstract Chemical-capture-mediated sensing has had a great impact on proteomic research. Toward this end, we demonstrate the chemical trapping of BSA by the reactive formyl functionality of a newly developed fluorescent nucleoside probe, formylphenothiazine-labeled-2′-deoxyuridine. The probe is capable of trapping BSA via Schiff base formation leading to fluorescence ‘switch-on’ sensing with a large hypsochromic shift of ca. 100 nm. The α-amylase does not show any significant change in fluorescence response, demonstrating the efficiency of the probe in selective sensing of BSA. Docking studies suggest the preferential interaction of the phenothiazinylcarbaldehyde-labeled dU with the residual amino acids in site I of the BSA protein as compared to site II.

Authors

Institutions

Publication Details

Journal
Synlett
Published
2024-10-07
DOI
https://doi.org/10.1055/a-2435-6207
Citations
2
Primary Topic
Protein Interaction Studies and Fluorescence Analysis
Type
article
Field-Weighted Citation Impact
0.47
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Chemical Capture and Sensing of Bovine Serum Albumin with Phenothiazinylcarbaldehyde-Labeled 2′-Deoxyuridine

Subhendu Sekhar Bag, Yogesh S. Sanghvi, Anant R. Kapdi, Krishna Chaitanya Gunturu et al.
2 citations
Synlett
Protein Interaction Studies and Fluorescence Analysis
0.47
article

Chemical Capture and Sensing of Bovine Serum Albumin with Phenothiazinylcarbaldehyde-Labeled 2′-Deoxyuridine

Subhendu Sekhar Bag, Yogesh S. Sanghvi, Anant R. Kapdi, Krishna Chaitanya Gunturu, Rajesh Sahu
article en
2 citations

Abstract

Abstract Chemical-capture-mediated sensing has had a great impact on proteomic research. Toward this end, we demonstrate the chemical trapping of BSA by the reactive formyl functionality of a newly developed fluorescent nucleoside probe, formylphenothiazine-labeled-2′-deoxyuridine. The probe is capable of trapping BSA via Schiff base formation leading to fluorescence ‘switch-on’ sensing with a large hypsochromic shift of ca. 100 nm. The α-amylase does not show any significant change in fluorescence response, demonstrating the efficiency of the probe in selective sensing of BSA. Docking studies suggest the preferential interaction of the phenothiazinylcarbaldehyde-labeled dU with the residual amino acids in site I of the BSA protein as compared to site II.

SynlettVol. 36(07)
Indian Institute of Technology Guwahati (IN), Institute of Chemical Technology (IN), Swami Ramanand Teerth Marathwada University (IN), SRM University (IN)
Clean water and sanitation
Openalex Percentile: Top 35%
Protein Interaction Studies and Fluorescence Analysis
0.47
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.