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Keywords = PB1 β-hairpin

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13 pages, 2510 KiB  
Article
Sandwich-Type Electrochemical Aptasensor with Supramolecular Architecture for Prostate-Specific Antigen
by Anabel Villalonga, Raúl Díaz, Irene Ojeda, Alfredo Sánchez, Beatriz Mayol, Paloma Martínez-Ruiz, Reynaldo Villalonga and Diana Vilela
Molecules 2024, 29(19), 4714; https://doi.org/10.3390/molecules29194714 - 5 Oct 2024
Cited by 4 | Viewed by 1404
Abstract
A novel sandwich-type electrochemical aptasensor based on supramolecularly immobilized affinity bioreceptor was prepared via host–guest interactions. This method utilizes an adamantane-modified, target-responsive hairpin DNA aptamer as a capture molecular receptor, along with a perthiolated β-cyclodextrin (CD) covalently attached to a gold-modified electrode surface [...] Read more.
A novel sandwich-type electrochemical aptasensor based on supramolecularly immobilized affinity bioreceptor was prepared via host–guest interactions. This method utilizes an adamantane-modified, target-responsive hairpin DNA aptamer as a capture molecular receptor, along with a perthiolated β-cyclodextrin (CD) covalently attached to a gold-modified electrode surface as the transduction element. The proposed sensing strategy employed an enzyme-modified aptamer as the signalling element to develop a sandwich-type aptasensor for detecting prostate-specific antigen (PSA). To achieve this, screen-printed carbon electrodes (SPCEs) with electrodeposited reduced graphene oxide (RGO) and gold nanoferns (AuNFs) were modified with the CD derivative to subsequently anchor the adamantane-modified anti-PSA aptamer via supramolecular associations. The sensing mechanism involves the affinity recognition of PSA molecules on the aptamer-enriched electrode surface, followed by the binding of an anti-PSA aptamer–horseradish peroxidase complex as a labelling element. This sandwich-type arrangement produces an analytical signal upon the addition of H2O2 and hydroquinone as enzyme substrates. The aptasensor successfully detected the biomarker within a concentration range of 0.5 ng/mL to 50 ng/mL, exhibiting high selectivity and a detection limit of 0.11 ng/mL in PBS. Full article
(This article belongs to the Special Issue Nano-Functional Materials for Sensor Applications)
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11 pages, 1386 KiB  
Article
Functional Importance of the Hydrophobic Residue 362 in Influenza A PB1 Subunit
by Johnson Jor-Shing Chan, Yun-Sang Tang, Chun-Yeung Lo and Pang-Chui Shaw
Viruses 2023, 15(2), 396; https://doi.org/10.3390/v15020396 - 30 Jan 2023
Cited by 2 | Viewed by 1592
Abstract
PB1, acting as the catalytic subunit of the influenza polymerase, has numerous sequentially and structurally conserved regions. It has been observed that the slight modification of residues in PB1 would greatly affect the polymerase activity and even host adaptation ability. Here, we identified [...] Read more.
PB1, acting as the catalytic subunit of the influenza polymerase, has numerous sequentially and structurally conserved regions. It has been observed that the slight modification of residues in PB1 would greatly affect the polymerase activity and even host adaptation ability. Here, we identified a critical residue, 362M, on the polymerase activity and virus replication. By means of the minireplicon assay, we assured the importance of the hydrophobicity of PB1 362, and the possibility that the size and charge of the side chain might directly interfere with the polymerase function. We also proposed a hydrophobic core between the PA-arch and the PB1 β-hairpin motifs and showed the importance of the core to the polymerase function. Full article
(This article belongs to the Section Animal Viruses)
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