Skip to main content

Research Repository

Advanced Search

All Outputs (10)

Computational investigation of cis-1,4-polyisoprene binding to the latex-clearing protein LcpK30 (2024)
Journal Article
Abu Hassan, A., Hanževački, M., & Pordea, A. (2024). Computational investigation of cis-1,4-polyisoprene binding to the latex-clearing protein LcpK30. PLoS ONE, 19(5), Article e0302398. https://doi.org/10.1371/journal.pone.0302398

Latex clearing proteins (Lcps) catalyze the oxidative cleavage of the C = C bonds in cis-1,4-polyisoprene (natural rubber), producing oligomeric compounds that can be repurposed to other materials. The active catalytic site of Lcps is buried inside t... Read More about Computational investigation of cis-1,4-polyisoprene binding to the latex-clearing protein LcpK30.

Encapsulation of copper phenanthroline within horse spleen apoferritin: characterisation, cytotoxic activity and ability to retain temozolomide (2024)
Journal Article
Cassioli, M. L., Fay, M., Turyanska, L., Bradshaw, T. D., Thomas, N. R., & Pordea, A. (2024). Encapsulation of copper phenanthroline within horse spleen apoferritin: characterisation, cytotoxic activity and ability to retain temozolomide. RSC Advances, 14(20), 14008-14016. https://doi.org/10.1039/d3ra07430g

Protein capsules are promising drug delivery vehicles for cancer research therapies. Apoferritin (AFt) is a self-assembling 12 nm diameter hollow nanocage with many desirable features for drug delivery, however, control of drug retention inside the p... Read More about Encapsulation of copper phenanthroline within horse spleen apoferritin: characterisation, cytotoxic activity and ability to retain temozolomide.

Computationally driven design of an artificial metalloenzyme using supramolecular anchoring strategies of iridium complexes to alcohol dehydrogenase (2021)
Journal Article
Martins, F., Pordea, A., & Jäger, C. M. (2021). Computationally driven design of an artificial metalloenzyme using supramolecular anchoring strategies of iridium complexes to alcohol dehydrogenase. Faraday Discussions, 234, 315-335. https://doi.org/10.1039/d1fd00070e

Artificial metalloenzymes (ArMs) confer non-biological reactivities to biomolecules, whilst taking advantage of the biomolecular architecture in terms of their selectivity and renewable origin. In particular, the design of ArMs by the supramolecular... Read More about Computationally driven design of an artificial metalloenzyme using supramolecular anchoring strategies of iridium complexes to alcohol dehydrogenase.

Oxidation of cadaverine by putrescine oxidase from Rhodococcus erythropolis (2021)
Journal Article
Anyanwu, V. E., Hall, S. J., Stephens, G., & Pordea, A. (2021). Oxidation of cadaverine by putrescine oxidase from Rhodococcus erythropolis. Journal of Chemical Technology and Biotechnology, 96(10), 2950-2955. https://doi.org/10.1002/jctb.6851

BACKGROUND
Putrescine oxidase (EC 1.4.3.10) is of interest for the microbial production of unsubstituted platform nitrogen (N-)heterocycles, because it only requires inexpensive oxygen as co-substrate. Putrescine oxidase from Rhodococcus erythropoli... Read More about Oxidation of cadaverine by putrescine oxidase from Rhodococcus erythropolis.

Design of artificial metalloenzymes for the reduction of nicotinamide cofactors (2021)
Journal Article
Basle, M., Padley, H. A., Martins, F. L., Winkler, G. S., Jäger, C. M., & Pordea, A. (2021). Design of artificial metalloenzymes for the reduction of nicotinamide cofactors. Journal of Inorganic Biochemistry, 220, Article 111446. https://doi.org/10.1016/j.jinorgbio.2021.111446

Artificial metalloenzymes result from the insertion of a catalytically active metal complex into a biological scaffold, generally a protein devoid of other catalytic functionalities. As such, their design requires efforts to engineer substrate bindin... Read More about Design of artificial metalloenzymes for the reduction of nicotinamide cofactors.

Engineering of Thermovibrio ammonificans carbonic anhydrase mutants with increased thermostability (2019)
Journal Article
Parra-Cruz, R., Lau, P. L., Loh, H.-S., & Pordea, A. (2020). Engineering of Thermovibrio ammonificans carbonic anhydrase mutants with increased thermostability. Journal of Co2 Utilization, 37, 1-8. https://doi.org/10.1016/j.jcou.2019.11.015

Carbonic anhydrase can be used as an additive to improve the efficiency of carbon capture and utilisation processes, due to its ability to increase the rate of CO2 absorption into solvents. Successful industrial application requires robust carbonic a... Read More about Engineering of Thermovibrio ammonificans carbonic anhydrase mutants with increased thermostability.

Rational design of thermostable carbonic anhydrase mutants using molecular dynamics simulations (2018)
Journal Article
Parra-Cruz, R., Jäger, C. M., Lau, P. L., Gomes, R. L., & Pordea, A. (2018). Rational design of thermostable carbonic anhydrase mutants using molecular dynamics simulations. Journal of Physical Chemistry B, 122(36), 8526-8536. https://doi.org/10.1021/acs.jpcb.8b05926

The stability of enzymes is critical for their application in industrial processes, which generally require different conditions from the natural enzyme environment. Both rational and random protein engineering approaches have been used to increase s... Read More about Rational design of thermostable carbonic anhydrase mutants using molecular dynamics simulations.

Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase (2018)
Journal Article
Morra, S., & Pordea, A. (2018). Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase. Chemical Science, 9(38), 7447-7454. https://doi.org/10.1039/C8SC02371A

© The Royal Society of Chemistry. Chemo-enzymatic cascades of enzymes with transition metal catalysts can offer efficient synthetic strategies, but their development is challenging due to the incompatibility between proteins and transition metal comp... Read More about Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase.

Iron-catalyzed indolizine synthesis from pyridines, diazo compounds, and alkynes (2017)
Journal Article
Douglas, T., Pordea, A., & Dowden, J. (in press). Iron-catalyzed indolizine synthesis from pyridines, diazo compounds, and alkynes. Organic Letters, 19(23), https://doi.org/10.1021/acs.orglett.7b03252

The iron (III) catalyzed synthesis of indolizines from commercially available alkyne, pyridine, and diazo precursors is reported. This mild, expedient method is tolerant of various solvents and proceeds with as little as 0.25 mol % [Fe(TPP)Cl]. Signi... Read More about Iron-catalyzed indolizine synthesis from pyridines, diazo compounds, and alkynes.