biostudies-literatureYang XSpecial Funding Program of ShenZhen UniversityShenzhen Key Laboratory of Maternal and Child Health and Diseases1792-1805https://www.ebi.ac.uk/biostudies/studies/S-EPMC11897952biostudies-literatureUnknown11(3)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 thatACS biomaterials science & engineeringBiohybrid Nanosystem Fabricated with Marine Diatom <i>Thalassiosira pseudonana</i> for Uric Acid Detection.PMC11897952ZDSYS20230626091559006No.2024TBZZJH002Yang XXiong YWang BChen JYing MLong SfalseBiohybrid Nanosystem Fabricated with Marine Diatom <i>Thalassiosira pseudonana</i> for Uric Acid Detection.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 that2025-01-01T00:00:00Z2025 Mar2025-04-04T09:07:10.488Z2025-04-04T09:07:10.488ZS-EPMC118979523996732910.1021/acsbiomaterials.4c02312