Surface histidine mutations for the metal affinity purification of a β-carbonic anhydrase

Hoffmann, Katherine; Wood, Kaitlin M.; Labrum, Alysha D.; Lee, Dave K.; Bolinger, Ingmar M.; Konis, Mary E.; Blount, Adam G.; Prussia, Gregory A.; Schroll, Monica M.; Watson, J.

doi:10.1016/j.ab.2014.04.020

Cited by 2 publications

(2 citation statements)

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“…of phenolic compounds are also note worthy (Ambriz-Pérez et al 2016;Anantharaju et al 2016;George and Mabon 2000;Hanson et al 2002). These features are inarguably due to the presence of one or more hydroxyl functionality, which has potential to donate hydrogen, and abstract-free radical, coordinate with metal ions and amino acids (Del Prete et al 2017;Hoffmann et al 2014;Duthie et al 2000;Umar Lule and Xia 2005). In the context of β-CA1 inhibitory activity, it has been demonstrated that a subtle change in the core structure of phenolic compound leads to a significant change in the activity of β-CA1 enzyme (Davis et al 2011;Buchieri et al 2013).…”

Section: Introductionmentioning

confidence: 99%

Designing of phenol-based β−carbonic anhydrase1 inhibitors through QSAR, molecular docking, and MD simulation approach

2018

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Tuberculosis (Tb) is an airborne infectious disease caused by () has emerged as one of the potential targets for new antitubercular drug development. In this work, three-dimensional quantitative structure-activity relationships (3D-QSAR), molecular docking, and molecular dynamics (MD) simulation approaches were performed on a series of natural and synthetic phenol-based inhibitors. The developed 3D-QSAR model ( = 0.94, = 0.86, and pred_r = 0.74) indicated that the steric and electrostatic factors are important parameters to modulate the bioactivity of phenolic compounds. Based on this indication, we designed 72 new phenolic inhibitors, out of which two compounds (D25 and D50) effectively stabilized receptor and, thus, are potential candidates for new generation antitubercular drug discovery program.

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Section: Introductionmentioning

confidence: 99%

Designing of phenol-based β−carbonic anhydrase1 inhibitors through QSAR, molecular docking, and MD simulation approach

2018

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“…This is the first step toward developing a general method to engineer the protein surface to make it capable to bind a metal ion, such as nickel, and make possible it purification by a metal affinity chromatography. Compared with the published three chromatography techniques (cation-exchange, hydrophobic exchange and gel exclusion), metal affinity purification was a substantial improvement in time and resources 74 . Different from past studies 66 , Ozensoy et al prepared a new affinity gel for the purification of a-CAs with some modifications.…”

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confidence: 99%

A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization

Guler

Capasso

Supuran

2015

Journal of Enzyme Inhibition and Medicinal Chemistry

130

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In this paper, we reviewed the purification and characterization methods of the a-carbonic anhydrase (CA, EC 4.2.1.1) class. Six genetic families (a-, b-, g-, d-, z-and Z-CAs) all know to date, all encoding such enzymes in organisms widely distributed over the phylogenetic tree. Starting from the manuscripts published in the 1930s on the isolation and purification of a-CAs from blood and other tissues, and ending with the recent discovery of the last genetic family in protozoa, the Z-CAs, considered for long time an a-CA, we present historically the numerous and different procedures which were employed for obtaining these catalysts in pure form. a-CAs possess important application in medicine (as many human a-CA isoforms are drug targets) as well as biotechnological processes, in which the enzymes are ultimately used for CO 2 capture in order to mitigate the global warming effects due to greenhouse gases. Recently, it was discovered an involvement of CAs in cancerogenesis as well as infection caused by pathogenic agents such as bacteria, fungi and protozoa. Inhibition studies of CAs identified in the genome of the aforementioned organisms might lead to the discovery of innovative drugs with a novel mechanism of action.

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Surface histidine mutations for the metal affinity purification of a β-carbonic anhydrase

Cited by 2 publications

References 11 publications

Designing of phenol-based β−carbonic anhydrase1 inhibitors through QSAR, molecular docking, and MD simulation approach

Designing of phenol-based β−carbonic anhydrase1 inhibitors through QSAR, molecular docking, and MD simulation approach

A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization

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