Screening of β-hairpin peptide-engrafted 1,2,3-triazoles to identify APEH enzyme inhibitors

RSC Advances ◽  
2015 ◽  
Vol 5 (13) ◽  
pp. 9965-9972 ◽  
Author(s):  
A. Sandomenico ◽  
V. Celentano ◽  
L. D. D'Andrea ◽  
G. Palmieri ◽  
M. Ruvo
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors ◽  
Proteasome Activity ◽  
Inhibition Activity ◽  
Peptide Hydrolase

Peptide-engrafted triazoles, obtained via click chemistry, drive the inhibition activity toward Acyl Peptide Hydrolase (APEH), a modulator of the proteasome activity.

Use of Click-Chemistry in the Development of Peptidomimetic Enzyme Inhibitors

2014 ◽  
Vol 21 (13) ◽  
pp. 1467-1477 ◽  
Author(s):  
P. Fabbrizzi ◽  
G. Menchi ◽  
A. Guarna ◽  
A. Trabocchi
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors

Synthesis, Antimicrobial and β-Lactamase Enzyme Inhibition Activity of Some New Tetrazole Containing Maleamic and Phthaleamic Acid Derivatives

2019 ◽  
Vol 4 (3) ◽  
pp. 166-173
Author(s):  
Bhaurao P. Sathe ◽  
Harshal S. Oman ◽  
Naziya N.M.A. Rehman ◽  
Prashant P. Dixit ◽  
Arun S. Kharat ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Enzyme Inhibition ◽  
1H Nmr ◽  
13C Nmr ◽  
Enzyme Inhibitors ◽  
Inhibition Activity ◽  
Spectral Techniques

In the present study, two series of tetrazole containing maleamic (5a-h) and phthaleamic acid (5i-l) derivatives were synthesized and evaluated for their antimicrobial and β-lactamase enzyme inhibition activities. The synthesized compounds were characterized by IR, 1H NMR and 13C NMR spectral techniques. Among the screened compounds, the compound 5c, 5d, 5e, 5f, 5g and 5h have shown good antimicrobial activity. We further performed exploratory β-lactamase enzyme inhibitors studies on β-lactamase.

In Situ Click Chemistry:  Enzyme Inhibitors Made to Their Own Specifications

2004 ◽  
Vol 126 (40) ◽  
pp. 12809-12818 ◽  
Author(s):  
Roman Manetsch ◽  
Antoni Krasiński ◽  
Zoran Radić ◽  
Jessica Raushel ◽  
Palmer Taylor ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors

Methods of using click chemistry in the discovery of enzyme inhibitors

2007 ◽  
Vol 2 (11) ◽  
pp. 2655-2664 ◽  
Author(s):  
Rajavel Srinivasan ◽  
Junqi Li ◽  
Su Ling Ng ◽  
Karunakaran A Kalesh ◽  
Shao Q Yao
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors

Application of click chemistry towards an efficient synthesis of 1,2,3-1H-triazolyl glycohybrids as enzyme inhibitors

2011 ◽  
Vol 346 (1) ◽  
pp. 16-25 ◽  
Author(s):  
Namarata Anand ◽  
Natasha Jaiswal ◽  
Sarvesh Kumar Pandey ◽  
A.K. Srivastava ◽  
Rama P. Tripathi
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors ◽  
Efficient Synthesis

scholarly journals Recent Advances about the Applications of Click Reaction in Chemical Proteomics

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5368
Author(s):  
Tingting Yao ◽  
Xiaowei Xu ◽  
Rong Huang
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors ◽  
Click Reaction ◽  
Monolithic Column ◽  
Protein Composition ◽  
Protein Profiling ◽  
High Yield ◽  
Dynamic Interactions ◽  
Chemical Proteomics ◽  
Analytical Approaches

Despite significant advances in biological and analytical approaches, a comprehensive portrait of the proteome and its dynamic interactions and modifications remains a challenging goal. Chemical proteomics is a growing area of chemical biology that seeks to design small molecule probes to elucidate protein composition, distribution, and relevant physiological and pharmacological functions. Click chemistry focuses on the development of new combinatorial chemical methods for carbon heteroatom bond (C-X-C) synthesis, which have been utilized extensively in the field of chemical proteomics. Click reactions have various advantages including high yield, harmless by-products, and simple reaction conditions, upon which the molecular diversity can be easily and effectively obtained. This paper reviews the application of click chemistry in proteomics from four aspects: (1) activity-based protein profiling, (2) enzyme-inhibitors screening, (3) protein labeling and modifications, and (4) hybrid monolithic column in proteomic analysis.

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