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

被引：0

作者：

Tolicheva, O. A. ^{[1
]}

Bidzhieva, M. S. ^{[1
]}

Kasatskiy, P. S. ^{[1
]}

Marina, V. I. ^{[2
,3
]}

Sergiev, P. V. ^{[2
,3
]}

Konevega, A. L. ^{[1
,4
,5
]}

Paleskava, A. ^{[1
,4
]}

机构：

[1] Kurchatov Inst, Petersburg Nucl Phys Inst, Natl Res Ctr, Gatchina 188300, Russia

[2] Skolkovo Inst Sci & Technol, Skolkovo 121205, Russia

[3] Moscow MV Lomonosov State Univ, Moscow 119991, Russia

[4] Peter Great St Petersburg Polytech Univ, St Petersburg 195251, Russia

[5] Kurchatov Inst, Natl Res Ctr, Moscow 123182, Russia

来源：

NANOBIOTECHNOLOGY REPORTS | 2024年 / 19卷 / 03期

基金：

俄罗斯科学基金会;

关键词：

TRANSFER-RNA MOVEMENT; MESSENGER-RNA; A-SITE; RIBOSOME; TRANSLOCATION; NUCLEOTIDES; HYDROLYSIS; MECHANISMS; MACROLIDE; PROTEINS;

D O I：

10.1134/S263516762460127X

中图分类号：

TB3 [工程材料学];

学科分类号：

0805 ; 080502 ;

摘要：

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 epsilon NH2-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.

引用

页码：423 / 431

页数：9