Compounds > n-n--bis(salicylidene)-1-6-hexanediamine

n-n--bis(salicylidene)-1-6-hexanediamine and Neoplasms

n-n--bis(salicylidene)-1-6-hexanediamine has been researched along with Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for n-n--bis(salicylidene)-1-6-hexanediamine and Neoplasms

Article	Year
Salen and tetrahydrosalen derivatives act as effective inhibitors of the tumor-associated carbonic anhydrase XII--a new scaffold for designing isoform-selective inhibitors. Bioorganic & medicinal chemistry letters, 2013, Dec-15, Volume: 23, Issue:24 Salen and tetrahydrosalen derivatives possess metal-chelating properties and have been used as ligands in organic synthesis and as scaffolds for developing therapeutic agents. Fourteen such compounds were synthesized in order to explore their ability to inhibit the zinc enzyme carbonic anhydrase (CA, EC 4.2.1.1). Human (h) isoforms hCA I, hCA II, hCA IX and hCA XII were included in the investigation. Several aliphatic and aromatic spacers were introduced between the two chelating groups from salen/tetrahydrosalen in order to explore a diverse chemical space for designing CA inhibitors, which incorporate both phenol and polyamine fragments in their molecule. Some of these compounds showed CA inhibitory activity in the low micromolar-nanomolar range and a pronounced selectivity for inhibiting an isoform over-expressed in hypoxic tumors, hCA XII, over hCA I, II and IX. Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Drug Design; Enzyme Activation; Ethylenediamines; Humans; Neoplasms; Phenol; Polyamines; Protein Binding; Protein Isoforms; Structure-Activity Relationship	2013

Article

Year

Salen and tetrahydrosalen derivatives act as effective inhibitors of the tumor-associated carbonic anhydrase XII--a new scaffold for designing isoform-selective inhibitors.

Bioorganic & medicinal chemistry letters, 2013, Dec-15, Volume: 23, Issue:24

Salen and tetrahydrosalen derivatives possess metal-chelating properties and have been used as ligands in organic synthesis and as scaffolds for developing therapeutic agents. Fourteen such compounds were synthesized in order to explore their ability to inhibit the zinc enzyme carbonic anhydrase (CA, EC 4.2.1.1). Human (h) isoforms hCA I, hCA II, hCA IX and hCA XII were included in the investigation. Several aliphatic and aromatic spacers were introduced between the two chelating groups from salen/tetrahydrosalen in order to explore a diverse chemical space for designing CA inhibitors, which incorporate both phenol and polyamine fragments in their molecule. Some of these compounds showed CA inhibitory activity in the low micromolar-nanomolar range and a pronounced selectivity for inhibiting an isoform over-expressed in hypoxic tumors, hCA XII, over hCA I, II and IX.

Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Drug Design; Enzyme Activation; Ethylenediamines; Humans; Neoplasms; Phenol; Polyamines; Protein Binding; Protein Isoforms; Structure-Activity Relationship

2013