Crystallographic approach to fragment-based hit discovery against Schistosoma mansoni purine nucleoside phosphorylase Article Swipe
Muhammad Faheem
,
Napoleão Fonseca Valadares
,
J. Brandão-Neto
,
Dom Bellini
,
P.M. Collins
,
Nicholas M. Pearce
,
Louise E. Bird
,
J.R. Torini
,
Raymond J. Owens
,
H.M. Pereira
,
F. von Delft
,
J.A.R.G. Barbosa
·
YOU?
·
· 2021
· Open Access
·
· DOI: https://doi.org/10.1042/bcj20210041
YOU?
·
· 2021
· Open Access
·
· DOI: https://doi.org/10.1042/bcj20210041
Several Schistosoma species cause Schistosomiasis, an endemic disease in 78 countries that is ranked second amongst the parasitic diseases in terms of its socioeconomic impact and human health importance. The drug recommended for treatment by the WHO is praziquantel (PZQ), but there are concerns associated with PZQ, such as the lack of information about its exact mechanism of action, its high price, its effectiveness — which is limited to the parasite's adult form — and reports of resistance. The parasites lack the de novo purine pathway, rendering them dependent on the purine salvage pathway or host purine bases for nucleotide synthesis. Thus, the Schistosoma purine salvage pathway is an attractive target for the development of necessary and selective new drugs. In this study, the purine nucleotide phosphorylase II (PNP2), a new isoform of PNP1, was submitted to a high-throughput fragment-based hit discovery using a crystallographic screening strategy. PNP2 was crystallized and crystals were soaked with 827 fragments, a subset of the Maybridge 1000 library. X-ray diffraction data was collected and structures were solved. Out of 827-screened fragments we have obtained a total of 19 fragments that show binding to PNP2. Fourteen of these fragments bind to the active site of PNP2, while five were observed in three other sites. Here we present the first fragment screening against PNP2.
Related Topics
Concepts
Purine nucleoside phosphorylase
Nucleotide salvage
Schistosoma mansoni
Purine
Drug discovery
Biology
Nucleotide
Virtual screening
Computational biology
Biochemistry
Enzyme
Schistosomiasis
Immunology
Gene
Helminths
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1042/bcj20210041
- OA Status
- hybrid
- Cited By
- 1
- References
- 38
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3199827934
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W3199827934Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1042/bcj20210041Digital Object Identifier
- Title
-
Crystallographic approach to fragment-based hit discovery against Schistosoma mansoni purine nucleoside phosphorylaseWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2021Year of publication
- Publication date
-
2021-09-16Full publication date if available
- Authors
-
Muhammad Faheem, Napoleão Fonseca Valadares, J. Brandão-Neto, Dom Bellini, P.M. Collins, Nicholas M. Pearce, Louise E. Bird, J.R. Torini, Raymond J. Owens, H.M. Pereira, F. von Delft, J.A.R.G. BarbosaList of authors in order
- Landing page
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https://doi.org/10.1042/bcj20210041Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
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hybridOpen access status per OpenAlex
- OA URL
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https://doi.org/10.1042/bcj20210041Direct OA link when available
- Concepts
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Purine nucleoside phosphorylase, Nucleotide salvage, Schistosoma mansoni, Purine, Drug discovery, Biology, Nucleotide, Virtual screening, Computational biology, Biochemistry, Enzyme, Schistosomiasis, Immunology, Gene, HelminthsTop concepts (fields/topics) attached by OpenAlex
- Cited by
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1Total citation count in OpenAlex
- Citations by year (recent)
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2023: 1Per-year citation counts (last 5 years)
- References (count)
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38Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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