210832-86-3
Chemical Structure
BADAN
- CAS No.: 210832-86-3
- Formula:C14H14BrNO
- Molecular Weight:292.17
IUPAC Name: 2-bromo-1-(3-fluorobicyclo[1.1.1]pentan-1-yl)ethan-1-one
InChIKey: ZEIHZWQYRTVVMA-UHFFFAOYSA-N
SMILES: O=C(CBr)C1=CC=C2C=C(N(C)C)C=CC2=C1
Biological Activity: BADAN is a thiol-reactive, environment-sensitive fluorescent probe used for site-specific labeling of protein cysteine residues to detect protein topology, local polarity, protein-lipid interactions, and conformational changes. The bromoacetyl group of BADAN covalently binds to cysteine thiols, and its fluorescence originates from the intramolecular charge transfer (ICT) excited state. The emission peak position varies with the polarity of the surrounding medium: it blue-shifts to approximately 488 nm in nonpolar environments (such as the hydrophobic core of lipid bilayers) and red-shifts to approximately 496-507 nm in polar environments (such as aqueous phases), independent of enzymes, pH, or membrane potential. Ex = 380-402 nm; Em = 400-600 nm[1][2][3][4][5].
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BADAN | BADAN is a thiol-reactive, environment-sensitive fluorescent probe used for site-specific labeling of protein cysteine residues to detect protein topology, local polarity, protein-lipid interactions, and conformational changes. The bromoacetyl group of BADAN covalently binds to cysteine thiols, and its fluorescence originates from the intramolecular charge transfer (ICT) excited state. The emission peak position varies with the polarity of the surrounding medium: it blue-shifts to approximately 488 nm in nonpolar environments (such as the hydrophobic core of lipid bilayers) and red-shifts to approximately 496-507 nm in polar environments (such as aqueous phases), independent of enzymes, pH, or membrane potential. Ex = 380-402 nm; Em = 400-600 nm. | |||||||||||||||||||||
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- [1]. Pospíšil P, et al. Fluorescence quenching of (dimethylamino)naphthalene dyes Badan and Prodan by tryptophan in cytochromes P450 and micelles. The journal of physical chemistry. B. 2014 Aug 28;118(34):10085-91.
- [2]. Koehorst RB, et al. Site-directed fluorescence labeling of a membrane protein with BADAN: probing protein topology and local environment. Biophysical journal. 2008 May 15;94(10):3945-55.
- [3]. Koehorst RB, et al. Profiling of dynamics in protein-lipid-water systems: a time-resolved fluorescence study of a model membrane protein with the label BADAN at specific membrane depths. European biophysics journal : EBJ. 2010 Mar;39(4):647-56.
- [4]. Tsalkova TN, et al. Mechanism of interactions of α-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe. Biochemistry. 2008;47(43):11324-11336.
- [5]. Schindel C, et al. Interaction of Escherichia coli hemolysin with biological membranes. A study using cysteine scanning mutagenesis. European journal of biochemistry. 2001 Feb;268(3):800-8. [Content Brief]
Keywords
