Paper Details 
Original Abstract of the Article :
We report the cloning, purification and characterization of the full domain of carbonic anhydrase (CA, EC 4.2.1.1) from Plasmodium falciparum, which incorporates 358 amino acid residues (from 181 to 538, in the sequence of this 600 amino acid long protein), called PfCAdom. The enzyme, which belongs ...See full text at original site
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引用元:
https://doi.org/10.1016/j.bmcl.2016.07.060

データ提供:米国国立医学図書館(NLM)

Unveiling the Secrets of Carbonic Anhydrase in Malaria

This research takes us into the fascinating world of malaria, specifically exploring the activity of carbonic anhydrase (CA), a crucial enzyme involved in various cellular processes. The researchers focused on a specific type of CA, called η-CA, found in Plasmodium falciparum, the parasite responsible for the most severe form of malaria. Their investigation involved cloning, expressing, and purifying this enzyme, revealing its intricate structure and catalytic activity. The study also delved into the potential of sulfonamides, a class of drugs known to inhibit CA, to target this enzyme in malaria. These findings offer promising insights into the development of novel anti-malarial therapies.

Targeting Carbonic Anhydrase in Malaria

The study reveals the potential of PfCAdom, the full domain of the η-CA enzyme in Plasmodium falciparum, as a target for anti-malarial drugs. The researchers demonstrated that this enzyme possesses significant catalytic activity, making it an attractive target for therapeutic intervention. While sulfonamide inhibitors showed weaker activity against PfCAdom compared to a truncated form of the enzyme, further investigation may lead to the development of more potent inhibitors that can effectively target this enzyme.

A Promising Avenue for Malaria Treatment

This research offers a glimmer of hope in the battle against malaria. The study suggests that targeting the η-CA enzyme in Plasmodium falciparum could be a promising strategy for developing new anti-malarial therapies. Further investigation is needed to explore the potential of sulfonamides and other drug candidates to effectively inhibit this crucial enzyme, ultimately contributing to the fight against this deadly disease.

Dr.Camel's Conclusion

This study is like a treasure hunt through the complex world of malaria, uncovering a hidden treasure in the form of PfCAdom, a crucial enzyme that might hold the key to developing new anti-malarial therapies. The researchers have carefully mapped the enzyme's structure and activity, paving the way for future research to explore the potential of sulfonamides and other drug candidates to effectively target this crucial enzyme. This study reminds us that even in the harshest of environments, like the desert of malaria, there is always hope for finding solutions.

Date :
  1. Date Completed 2017-07-26
  2. Date Revised 2017-11-22
Further Info :

Pubmed ID

27485387

DOI: Digital Object Identifier

10.1016/j.bmcl.2016.07.060

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SNS
PICO Info
in preparation
Languages

English

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