scholarly journals In vivo modulation of ubiquitin chains by N-methylated non-proteinogenic cyclic peptides

2021 ◽  
Author(s):  
Joseph M. Rogers ◽  
Mickal Nawatha ◽  
Betsegaw Lemma ◽  
Ganga B. Vamisetti ◽  
Ido Livneh ◽  
...  
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Cyclic Peptides ◽  
In Cells

Cyclic peptides containing unnatural amino acids can modulate Lys-48 ubiquitin chains in cells and animals.

Engineering an acetyllysine reader with photocrosslinking amino acid for interactome profiling

2021 ◽  
Author(s):  
Babu Sudhamalla ◽  
Anirban Roy ◽  
Soumen Barman ◽  
Jyotirmayee Padhan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Interactions ◽  
Unnatural Amino Acids ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Powerful Approach

The site-specific installation of light-activable crosslinker unnatural amino acids offers a powerful approach to trap transient protein-protein interactions both in vitro and in vivo. Herein, we engineer a bromodomain to...

Molecular Design and Synthesis of Artificial Ion Channels Based on Cyclic Peptides Containing Unnatural Amino Acids

2001 ◽  
Vol 66 (9) ◽  
pp. 2978-2989 ◽  
Author(s):  
Hitoshi Ishida ◽  
Zhi Qi ◽  
Masahiro Sokabe ◽  
Kiyoshi Donowaki ◽  
Yoshihisa Inoue
Keyword(s):  
Amino Acids ◽  
Ion Channels ◽  
Unnatural Amino Acids ◽  
Cyclic Peptides ◽  
Molecular Design ◽  
Design And Synthesis

scholarly journals Bases alternatives et organismes synthétiques

2018 ◽  
Vol 34 (2) ◽  
pp. 179-182 ◽  
Author(s):  
Bertrand Jordan
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Double Helix ◽  
Dna Double Helix

Alternative bases that can fit into the DNA double helix have now been used in vivo to direct the synthesis of proteins incorporating unnatural amino acids. This bioengineering feat is significant at both the conceptual and the practical levels

Oxidized amino acids in the urine of aging rats: potential markers for assessing oxidative stress in vivo

1999 ◽  
Vol 276 (1) ◽  
pp. R128-R135 ◽  
Author(s):  
Christiaan Leeuwenburgh ◽  
Polly A. Hansen ◽  
John O. Holloszy ◽  
Jay W. Heinecke
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Amino Acids ◽  
Exercise Training ◽  
Protein Oxidation ◽  
Unnatural Amino Acids ◽  
Antioxidant Therapy ◽  
Gas Chromatography Mass Spectrometry ◽  
Aging Rats

Oxidative damage of proteins has been implicated in disease and aging. In vitro studies demonstrate that two unnatural amino acids, o,o′-dityrosine and o-tyrosine, are stable markers of protein oxidation. We have investigated the possibility that assaying these compounds in urine could provide a noninvasive way to determine levels of protein oxidation in vivo. Isotope dilution gas chromatography-mass spectrometry was used to quantify levels of o,o′-dityrosine and o-tyrosine in skeletal muscle and urine of aging rats subjected to two interventions: 1) dietary antioxidant supplementation and 2) exercise training. In both sedentary rats and exercise-trained rats, antioxidant therapy reduced levels of protein-bound o,o′-dityrosine in skeletal muscle. In contrast, antioxidant therapy or exercise training minimally affected o-tyrosine levels in this tissue. Levels of the oxidized amino acids in urine samples mirrored those of skeletal muscle proteins. Quantification of the levels of oxidized amino acids in urine may thus serve as a noninvasive measure of oxidative stress in vivo because they change in parallel with levels of protein-bound oxidized amino acids in skeletal muscle.

Sign in / Sign up

Export Citation Format

Share Document