Peptide Derivatives Containing Two Trifunctional Amino Acids. II

1955 ◽  
Vol 77 (3) ◽  
pp. 750-751 ◽  
Author(s):  
R. F. Fischer ◽  
R. R. Whetstone
Keyword(s):  
Amino Acids ◽  
Peptide Derivatives

Thia-analogues of amino acids synthesis of peptide derivatives containing 3-thia-analogues of amino acids

Amino Acids ◽  
1992 ◽  
Vol 3 (1) ◽  
pp. 105-118 ◽  
Author(s):  
P. Hermann ◽  
H. Baumann ◽  
Ch. Herrnstadt ◽  
D. Glanz
Keyword(s):  
Amino Acids ◽  
Peptide Derivatives

scholarly journals Free radical destruction of hydroxyl-containing amino acids

2019 ◽  
pp. 3-13
Author(s):  
Anastasia A. Sladkova ◽  
Irina P. Edimecheva ◽  
Anna A. Sosnovskaya ◽  
Oleg I. Shadyro
Keyword(s):  
Amino Acids ◽  
Free Radical ◽  
Side Chain ◽  
Free Radical Processes ◽  
Peptide Derivatives ◽  
Novel Approaches ◽  
Radical Processes ◽  
Subsequent Decomposition ◽  
Reducing Properties

А new way of the free radical ROS- and HOCl-induced destruction of serine, threonine, and their peptide derivatives due to the nitrogen-centered radicals formation and their subsequent decomposition with the side chain elimination has been established. It has been shown that substances with reducing properties are inhibitors of this process, while oxygen does not affect the probability of its occurrence. The data obtained are relevant for the development of novel approaches to the search for effective free radical processes regulators.

scholarly journals α-Hydrogen Abstraction by •OH and •SH Radicals from Amino Acids and Their Peptide Derivatives

2016 ◽  
Vol 12 (4) ◽  
pp. 1606-1613 ◽  
Author(s):  
Bun Chan ◽  
Amir Karton ◽  
Christopher J. Easton ◽  
Leo Radom
Keyword(s):  
Amino Acids ◽  
Hydrogen Abstraction ◽  
Peptide Derivatives

Peptide Derivatives Containing Two Trifunctional Amino Acids

1954 ◽  
Vol 76 (20) ◽  
pp. 5076-5080 ◽  
Author(s):  
R. F. Fischer ◽  
R. R. Whetstone
Keyword(s):  
Amino Acids ◽  
Peptide Derivatives

Antimetastatic effect of synthetic Glu-lle-Leu-Asp- Val peptide derivatives containing D-amino acids

1997 ◽  
Vol 8 (7) ◽  
pp. 702-707 ◽  
Author(s):  
Yoshihisa Kaneda ◽  
Yoko Yamamoto ◽  
Naoki Okada ◽  
Yasuo Tsutsumi ◽  
Shinsaku Nakagawa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antimetastatic Effect ◽  
Peptide Derivatives

scholarly journals Modification and de novo design of non-ribosomal peptide synthetases (NRPS) using specific assembly points within condensation domains

2018 ◽  
Author(s):  
Kenan A. J. Bozhüyük ◽  
Annabell Linck ◽  
Andreas Tietze ◽  
Frank Wesche ◽  
Sarah Nowak ◽  
...  
Keyword(s):  
Amino Acids ◽  
De Novo ◽  
Covalent Binding ◽  
Efficient Production ◽  
Diverse Range ◽  
Peptide Synthetases ◽  
Catalytically Active ◽  
Peptide Derivatives ◽  
Natural Amino Acids ◽  
Exchange Unit

AbstractMany important natural products are produced by non-ribosomal peptide synthetases (NRPSs) 1.These giant enzyme machines activate amino acids in an assembly line fashion in which a set of catalytically active domains is responsible for the section, activation, covalent binding and connection of a specific amino acid to the growing peptide chain 1,2. Since NRPS are not restricted to the incorporation of the 20 proteinogenic amino acids, their efficient manipulation would give access to a diverse range of peptides available biotechnologically. Here we describe a new fusion point inside condensation (C) domains of NRPSs that enables the efficient production of peptides, even containing non-natural amino acids, in yields higher than 280 mg/L. The technology called eXchange Unit 2.0 (XU2.0) also allows the generation of targeted peptide libraries and therefore might be suitable for the future identification of bioactive peptide derivatives for pharmaceutical and other applications.

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