Abstract
Forming a stable complex is a prerequisite for intramolecular charge transfer (ICT) probe to recognize proteins. Herein, a human serum albumin (HSA) structure-based fluorescent probe DNPM was fabricated successfully with fully considering its binding to the primary sites in HSA. Molecular simulation was used to assist the probe design. Two ICT ligands DNPM and MPM were initially designed. Both DNPM and MPM had favorable HSA binding abilities, but only DNPM had a satisfactory HSA sensitivity. Electromagnetic coupling played a key role in DNPM fluorescence enhancement. Due to the electromagnetic environment difference in protein structure, DNPM only exhibited strong sensitivity to serum albumins. DNPM could bind to Sudlow site I and site II in HSA but could not be displaced from its binding sites by common site specific drugs (e.g. phenylbutazone and ibuprofen). Besides, DNPM exhibited great potential for illumining serum albumin in living cells. The results provided a beneficial approach for designing and synthesizing high sensitive and selective fluorescent probes for proteins.
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