A cysteine-specific fluorescent switch for monitoring oxidative stress and quantification of aminoacylase-1 in blood serum

  • H. A. Anila
  • , Firoj Ali
  • , Shilpi Kushwaha
  • , Nandaraj Taye
  • , Samit Chattopadhyay
  • , Amitava Das

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

Reagents that allows detection and monitoring of crucial biomarkers with luminescence ON response have significance in clinical diagnostics. A new coumarin derivative is reported here, which could be used for specific and efficient chemodosimetric detection of cysteine, an important biomarker. The probe is successfully used for studying the biochemical transformation of N-acetylcysteine, a commonly prescribed Cys supplement drug to Cys by aminoacylase-1 (ACY-1), an important and endogenous mammalian enzyme. The possibility of using this reagent for quantification of ACY-1 in blood serum samples is also explored. Nontoxic nature and cell membrane permeability are key features of this probe and are ideally suited for imaging intracellular Cys in normal and cancerous cell lines. Our studies have also revealed that this reagent could be utilized as a redox switch to monitor the hydrogenperoxide-induced oxidative stress in living SW480 cell lines. Peroxide-mediated cysteine oxidation has a special significance for understanding the cellular-signaling events.

Original languageEnglish
Pages (from-to)12161-12168
Number of pages8
JournalAnalytical Chemistry
Volume88
Issue number24
DOIs
StatePublished - 20 Dec 2016
Externally publishedYes

Fingerprint

Dive into the research topics of 'A cysteine-specific fluorescent switch for monitoring oxidative stress and quantification of aminoacylase-1 in blood serum'. Together they form a unique fingerprint.

Cite this