Separation of Short Fluorescently Labeled Peptides by Gel Electrophoresis for an In Vitro Translation Study

The development of simple, readily available, and sensitive methods for studying bacterial protein synthesis is an important fundamental and applied task. We recently demonstrated the possibility of visualizing short BODIPY-labeled phenylalanine- and leucine-containing peptides using urea-polyacryla...

Full description

Saved in:
Bibliographic Details
Published inNanobiotechnology Reports (Online) Vol. 19; no. 3; pp. 423 - 431
Main Authors Tolicheva, O. A., Bidzhieva, M. S., Kasatskiy, P. S., Marina, V. I., Sergiev, P. V., Konevega, A. L., Paleskava, A.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 2024
Springer Nature B.V
Subjects
Amino acids
Chemistry and Materials Science
Electrophoresis
In vitro methods and tests
Industrial and Production Engineering
Leucine
Lysine
Machines
Manufacturing
Materials Science
Nanobiology and Genetics
Nanotechnology
Omics Technologies
Peptides
Phenylalanine
Polyacrylamide
Processes
Protein synthesis
Valine
Online AccessGet full text

Cover

More Information
Summary:The development of simple, readily available, and sensitive methods for studying bacterial protein synthesis is an important fundamental and applied task. We recently demonstrated the possibility of visualizing short BODIPY-labeled phenylalanine- and leucine-containing peptides using urea-polyacrylamide gel electrophoresis under denaturing conditions. In this work, we expand the range of test sequences and included peptides with valine, lysine, and the modified amino acid εNH 2 -DOTA-lysine. The described method can also be used to study the mechanism of translation inhibition, as shown by elaboration of the specific action of the antibiotics etamycin A and viomycin.
ISSN:2635-1676
1995-0780
2635-1684
1995-0799
DOI:10.1134/S263516762460127X