{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang X"],"funding":["Special Funding Program of ShenZhen University","Shenzhen Key Laboratory of Maternal and Child Health and Diseases"],"pagination":["1792-1805"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11897952"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(3)"],"pubmed_abstract":["Due to the intense demand for low-cost, environmentally friendly, and stable uric acid (UA) detection methods, a novel biosensing nanosystem made with marine diatom was studied. Reduced by live diatom (<i>Thalassiosira pseudonana</i>), metallic nanoparticles (Cu<sub><i>X</i></sub>) were hybridized with the heteronanostructure (Diatom frustule, DF), showing peroxidase activity 2.66-fold over horseradish peroxidase (HRP). To immobilize the enzyme directionally with increasing loading amounts, silaffin peptides (R<sub>5</sub> and T<sub>8</sub>) were designed for tagging the urate oxidase (UoX). The enzyme loading on DF of tagged UoX was 1.76-fold (R<sub>5</sub>) and 1.54-fold (T<sub>8</sub>) that of untagged UoX. The activity of immobilized UoX-R<sub>5</sub> was 5.29-11.76-fold more than that"],"journal":["ACS biomaterials science & engineering"],"pubmed_title":["Biohybrid Nanosystem Fabricated with Marine Diatom &lt;i&gt;Thalassiosira pseudonana&lt;/i&gt; for Uric Acid Detection."],"pmcid":["PMC11897952"],"funding_grant_id":["ZDSYS20230626091559006","No.2024TBZZJH002"],"pubmed_authors":["Yang X","Xiong Y","Wang B","Chen J","Ying M","Long S"],"additional_accession":[]},"is_claimable":false,"name":"Biohybrid Nanosystem Fabricated with Marine Diatom &lt;i&gt;Thalassiosira pseudonana&lt;/i&gt; for Uric Acid Detection.","description":"Due to the intense demand for low-cost, environmentally friendly, and stable uric acid (UA) detection methods, a novel biosensing nanosystem made with marine diatom was studied. Reduced by live diatom (<i>Thalassiosira pseudonana</i>), metallic nanoparticles (Cu<sub><i>X</i></sub>) were hybridized with the heteronanostructure (Diatom frustule, DF), showing peroxidase activity 2.66-fold over horseradish peroxidase (HRP). To immobilize the enzyme directionally with increasing loading amounts, silaffin peptides (R<sub>5</sub> and T<sub>8</sub>) were designed for tagging the urate oxidase (UoX). The enzyme loading on DF of tagged UoX was 1.76-fold (R<sub>5</sub>) and 1.54-fold (T<sub>8</sub>) that of untagged UoX. The activity of immobilized UoX-R<sub>5</sub> was 5.29-11.76-fold more than that","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2025-04-04T09:07:10.488Z","creation":"2025-04-04T09:07:10.488Z"},"accession":"S-EPMC11897952","cross_references":{"pubmed":["39967329"],"doi":["10.1021/acsbiomaterials.4c02312"]}}