Selective labeling of tag-fused protein by tryptophan-sensitized luminescence of a terbium complex.

نویسندگان

  • Tasuku Hirayama
  • Masayasu Taki
  • Atsushi Kodan
  • Hiroaki Kato
  • Yukio Yamamoto
چکیده

A Tb3+ complex with two di(2-picolyl)amine (DPA) moieties and an oligo-aspartate peptide containing a tryptophan residue have been designed as a new binding pair for use in protein labeling.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Development and Validation of a Terbium-Sensitized Luminescence Analytical Method for Deferiprone

A sensitive fluorometric method for the determination of deferiprone (DFP) based on the formation of a luminescent complex with Tb3+ ions in aqueous solutions is reported. The maximum excitation and emission wavelengths were 295 and 545 nm, respectively. The effects of various factors on the luminescence intensity of the system were investigated and optimized, then under the optimum conditions,...

متن کامل

Development and Validation of a Terbium-Sensitized Luminescence Analytical Method for Deferiprone

A sensitive fluorometric method for the determination of deferiprone (DFP) based on the formation of a luminescent complex with Tb3+ ions in aqueous solutions is reported. The maximum excitation and emission wavelengths were 295 and 545 nm, respectively. The effects of various factors on the luminescence intensity of the system were investigated and optimized, then under the optimum conditions,...

متن کامل

Development of a Simple and Sensitive Terbium Sensitized Fluorescence Method for Determination of Epinephrine and Norepinephrine in Serum

     A simple, rapid, selective and highly sensitive fluorimetric method for determination of two catecholamines, i.e. norepinephrine (NE) and epinephrine (EP), in serum samples was developed. The method is based on the fluorescence sensitization of terbium (Tb3+) by complexation with both catecholamines in the presence of lanthanum (La3+), as a co-cation, and in a Na...

متن کامل

Time-resolved luminescence resonance energy transfer imaging of protein-protein interactions in living cells.

Förster resonance energy transfer (FRET) with fluorescent proteins permits high spatial resolution imaging of protein-protein interactions in living cells. However, substantial non-FRET fluorescence background can obscure small FRET signals, making many potential interactions unobservable by conventional FRET techniques. Here we demonstrate time-resolved microscopy of luminescence resonance ene...

متن کامل

Genetically Encoded FRET-Sensor Based on Terbium Chelate and Red Fluorescent Protein for Detection of Caspase-3 Activity

This article describes the genetically encoded caspase-3 FRET-sensor based on the terbium-binding peptide, cleavable linker with caspase-3 recognition site, and red fluorescent protein TagRFP. The engineered construction performs two induction-resonance energy transfer processes: from tryptophan of the terbium-binding peptide to Tb(3+) and from sensitized Tb(3+) to acceptor--the chromophore of ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Chemical communications

دوره 22  شماره 

صفحات  -

تاریخ انتشار 2009