Biochemical and Biophysical Research Communications
Regular ArticlePharmacological Profile of a Non-peptidic Dual Inhibitor of Neutral Endopeptidase 24.11 and Endothelin-Converting Enzyme
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Cu(II)-N-benzyl-amino-1H-tetrazole complex immobilized on magnetic chitosan as a highly effective nanocatalyst for C-N coupling reactions
2021, Journal of Organometallic ChemistryCitation Excerpt :These compounds are playing an important role in medicinal/pharmacological chemistry, material science, explosives/propellants, coordination chemistry [1–7], and versatile scaffolds for the synthesis of N-containing compounds, as well as being effective bioactive compounds, antihypertensive drugs, peptidase inhibitors, anti-HIV and anticancer/antitumor agents [8–10]. For instance, losartan and its analogues used as antihypertensive drugs and/or the peptidase inhibitor CGS-26303 are the most significant drugs comprising tetrazole rings [9,11-13]. Furthermore, 1,5-disubstituted tetrazoles utilized as the bioisostere (bioequivalent) of cis-amide bonds in peptides, show similar physicochemical features and improved metabolic stability in living organisms [14].
Endothelin-Converting Enzyme-1 (ECE-1)
2013, Handbook of Proteolytic EnzymesProbing the antiamoebic and cytotoxicity potency of novel tetrazole and triazine derivatives
2012, European Journal of Medicinal ChemistryCitation Excerpt :Considering the need of a new molecule for the treatment of amoebiasis, we had synthesized a series of tetrazole and triazine based sulfonamide derivatives. The ability of tetrazole ring to serve as the bioequivalent (bioisostere) of the carboxylic acid group, often results in a dramatic enhancement in the in vitro and/or in vivo activity [17,18], and had been extensively studied in pharmaceutical industry [19,20]. Tetrazoles exhibit potential biological activities and the core ring is an important constituent of number of modern drugs [21–26].
Crystal structure of mycobacterium tuberculosis zinc-dependent metalloprotease-1 (Zmp1), a metalloprotease involved in pathogenicity
2011, Journal of Biological ChemistryCitation Excerpt :The residues present in this subsite are all hydrophobic with the exception, in NEP, of Met579 (Ala489/Val603 in Zmp1/ECE-1, respectively). The slight difference in volume and hydrophobicity of the S1′ site resulting from this single mutation may explain the moderate preference, for ECE-1, of inhibitors carrying a bulky hydrophobic group at the P1′ site (1, 47, 48). A similar behavior could be envisaged also for Zmp1, as its S1′ subsite is entirely hydrophobic.
Structure of human Endothelin-converting Enzyme I Complexed with Phosphoramidon
2009, Journal of Molecular BiologyEndothelin-1 (1-31): From chymase-dependent synthesis to cardiovascular pathologies
2008, Vascular Pharmacology