Literature DB >> 9029259

Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS).

A A Gershkovich1, V V Kholodovych.   

Abstract

A prospective class of intramolecular fluorescence energy transfer substrates (IFETS) is described. In contrast to the known chromogenic and fluorogenic substrates that are used widely in the scientific and medical research, IFETS allow to control the enzymatic cleavage at any point of the peptide chain and thus permit simultaneous studies of enzymes of different specificity. We discuss the main types of donor and acceptor, their advantages and drawbacks and the effectiveness of exited-state energy transfer between them. High sensitivity and selectivity of IFETS in the assay of proteinases was demonstrated. They prove to be a very useful and very promising instrument for enzymology and medicine.

Entities:  

Mesh:

Substances:

Year:  1996        PMID: 9029259     DOI: 10.1016/s0165-022x(96)00023-1

Source DB:  PubMed          Journal:  J Biochem Biophys Methods        ISSN: 0165-022X


  12 in total

1.  Using fluorogenic peptide substrates to assay matrix metalloproteinases.

Authors:  G B Fields
Journal:  Methods Mol Biol       Date:  2001

2.  Comparison of metalloproteinase protein and activity profiling.

Authors:  Orsi Giricz; Janelle L Lauer; Gregg B Fields
Journal:  Anal Biochem       Date:  2010-10-23       Impact factor: 3.365

Review 3.  The concept of λ-ratiometry in fluorescence sensing and imaging.

Authors:  Alexander P Demchenko
Journal:  J Fluoresc       Date:  2010-04-01       Impact factor: 2.217

4.  Interaction of heparin with internally quenched fluorogenic peptides derived from heparin-binding consensus sequences, kallistatin and anti-thrombin III.

Authors:  Daniel C Pimenta; Iseli L Nantes; Eduardo S de Souza; Bernard Le Bonniec; Amando S Ito; Ivarne L S Tersariol; Vitor Oliveira; Maria A Juliano; Luiz Juliano
Journal:  Biochem J       Date:  2002-09-01       Impact factor: 3.857

5.  General and specific solvent effects in optical spectra of ortho-aminobenzoic acid.

Authors:  Marcelo Takara; Amando Siuiti Ito
Journal:  J Fluoresc       Date:  2005-03       Impact factor: 2.217

6.  Ddi1-like protein from Leishmania major is an active aspartyl proteinase.

Authors:  María J Perteguer; Paulino Gómez-Puertas; Carmen Cañavate; Francehuli Dagger; Teresa Gárate; Elizabeth Valdivieso
Journal:  Cell Stress Chaperones       Date:  2012-08-30       Impact factor: 3.667

7.  Exploration of the one-bead one-compound methodology for the design of prolyl oligopeptidase substrates.

Authors:  Gemma Comellas; Zusanna Kaczmarska; Teresa Tarragó; Meritxell Teixidó; Ernest Giralt
Journal:  PLoS One       Date:  2009-07-13       Impact factor: 3.240

8.  Recognition of fungal protease activities induces cellular activation and eosinophil-derived neurotoxin release in human eosinophils.

Authors:  Yoshinori Matsuwaki; Kota Wada; Thomas A White; Linda M Benson; M Cristine Charlesworth; James L Checkel; Yoshinari Inoue; Kyoko Hotta; Jens U Ponikau; Christopher B Lawrence; Hirohito Kita
Journal:  J Immunol       Date:  2009-10-28       Impact factor: 5.422

9.  Highly sensitive intramolecularly quenched fluorogenic substrates for renin based on the combination of L-2-amino-3-(7-methoxy-4-coumaryl)propionic acid with 2,4-dinitrophenyl groups at various positions.

Authors:  Katherine Paschalidou; Ulf Neumann; Bernd Gerhartz; Chryssa Tzougraki
Journal:  Biochem J       Date:  2004-09-15       Impact factor: 3.857

10.  Fret studies of conformational changes in heparin-binding peptides.

Authors:  Eduardo Sérgio de Souza; Alberto H Katagiri; Luiz Juliano; Maria Aparecida Juliano; Daniel Carvalho Pimenta; Amando Siuiti Ito
Journal:  J Fluoresc       Date:  2014-04-11       Impact factor: 2.217

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.