scholarly journals Chirality Effects in Jet-Cooled Cyclic Dipeptides

2019 ◽  
pp. 63-87 ◽  
Author(s):  
Ariel Pérez-Mellor ◽  
Anne Zehnacker
Keyword(s):  
Cyclic Dipeptides

scholarly journals Diketopiperazine Gels: New Horizons from the Self-Assembly of Cyclic Dipeptides

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3376
Author(s):  
Marco Scarel ◽  
Silvia Marchesan
Keyword(s):  
Drug Discovery ◽  
Enzymatic Hydrolysis ◽  
Self Assembly ◽  
Biological Activities ◽  
Functional Materials ◽  
The Self ◽  
Cyclic Dipeptides ◽  
New Horizons ◽  
Concise Review

Cyclodipeptides (CDPs) or 2,5-diketopiperazines (DKPs) can exert a variety of biological activities and display pronounced resistance against enzymatic hydrolysis as well as a propensity towards self-assembly into gels, relative to the linear-dipeptide counterparts. They have attracted great interest in a variety of fields spanning from functional materials to drug discovery. This concise review will analyze the latest advancements in their synthesis, self-assembly into gels, and their more innovative applications.

scholarly journals Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme

2021 ◽  
Vol 2 (1) ◽  
pp. 230-240
Author(s):  
Christopher J. Harding ◽  
Emmajay Sutherland ◽  
Jane G. Hanna ◽  
Douglas R. Houston ◽  
Clarissa M. Czekster
Keyword(s):  
Independent Manner ◽  
Cyclic Dipeptides

Cyclodipeptide synthases recognize a minimalistic substrate to produce cyclic dipeptides in a tRNA-independent manner.

scholarly journals Production of Pyrazine Derivatives in the Radiolysis of Aqueous Solutions of the Cyclic Dipeptides

Nature ◽  
1961 ◽  
Vol 189 (4761) ◽  
pp. 302-302
Author(s):  
MATHILDE KLAND-ENGLISH ◽  
WARREN M. GARRISON
Keyword(s):  
Aqueous Solutions ◽  
Cyclic Dipeptides

scholarly journals Cyclo(valine–valine) inhibits Vibrio cholerae virulence gene expression

Microbiology ◽  
2014 ◽  
Vol 160 (6) ◽  
pp. 1054-1062 ◽  
Author(s):  
Amit Vikram ◽  
Vanessa M. Ante ◽  
X. Renee Bina ◽  
Qin Zhu ◽  
Xinyu Liu ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Virulence Factor ◽  
Inhibitory Activity ◽  
Virulence Gene ◽  
Side Chains ◽  
Cyclic Dipeptides ◽  
Virulence Gene Expression ◽  
Factor Production ◽  
Virulence Regulator ◽  
Virulence Factor Production

Vibrio cholerae has been shown to produce a cyclic dipeptide, cyclo(phenylalanine–proline) (cFP), that functions to repress virulence factor production. The objective of this study was to determine if heterologous cyclic dipeptides could repress V. cholerae virulence factor production. To that end, three synthetic cyclic dipeptides that differed in their side chains from cFP were assayed for virulence inhibitory activity in V. cholerae. The results revealed that cyclo(valine–valine) (cVV) inhibited virulence factor production by a ToxR-dependent process that resulted in the repression of the virulence regulator aphA. cVV-dependent repression of aphA was found to be independent of known aphA regulatory genes. The results demonstrated that V. cholerae was able to respond to exogenous cyclic dipeptides and implicated the hydrophobic amino acid side chains on both arms of the cyclo dipeptide scaffold as structural requirements for inhibitory activity. The results further suggest that cyclic dipeptides have potential as therapeutics for cholera treatment.

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