Ask about this productRelated genes to: DTNB Blocking Peptide
- Gene:
- DTNB NIH gene
- Name:
- dystrobrevin beta
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2p23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-11
- Date modifiied:
- 2016-10-05
Related products to: DTNB Blocking Peptide
Related articles to: DTNB Blocking Peptide
- The fabrication of SERS nanotags with efficient antibody loading and high signal enhancement remains a challenging task for combining surface-enhanced Raman spectroscopy (SERS) and lateral flow immunoassay (LFIA). In this study, bimetallic Au@PDA@Ag nanoparticles with a polydopamine (PDA)-based internal nanogap were synthesized and functionalized with anti-prolactin monoclonal antibodies to produce SERS nanotags. Here, polydopamine serves both as a spacer providing a nanogap between the core and the shell, and as a reaction layer to capture Raman reporter 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) within the nanogap. Regimes (conditions, protocols) for conjugating antibodies to Au@PDA@Ag were selected to preserve both the binding affinity for the target analyte and the Raman activity of the SERS nanotag. The SERS nanotag provides plasmonic absorption for visible colorimetric readout, as well as strong SERS signals for highly sensitive quantitative immunoassay. Measuring the Raman intensities of DTNB in the test zone after performing LFIA made it possible to determine prolactin with a detection limit of 0.2 ng/mL in the working range from 1 to 10 ng/mL. The achieved limit of detection was 10-fold lower than the LFIA coupled with colorimetric readout (4.7 ng/mL). The recoveries of prolactin from spiked serum samples were in the range of 70.2-82.6% with relative standard deviations of 2.3-6.8%. Overall, the Au@PDA@Ag nanotag demonstrated high stability, Raman activity, and specificity, indicating that the SERS nanotag with PDA-assisted internal nanogap is promising for use in SERS immunoassay of other target analytes. - Source: PubMed
Publication date: 2026/05/12
Serebrennikova Kseniya VKomova Nadezhda SZherdev Anatoly VDzantiev Boris B - Mussel foot proteins (Mfps) are renowned for their underwater adhesion, whereas their biotechnological potential for cutaneous wound repair remains largely underexplored. In this study, we identified and characterized a cysteine-rich mussel foot protein, Mfp6-1, from and investigated its therapeutic potential for wound healing. Sequence analysis showed that Mfp6-1 is enriched in cysteine (11.0%) and tyrosine (~16.5%). We successfully expressed recombinant Mfp6-1 (rMfp6-1) in . Structural prediction based on the mature peptide sequence suggested that rMfp6-1 adopts a relatively compact fold containing several short β-structural elements. In vitro assays demonstrated that rMfp6-1 possesses antioxidant activity in the 2,2-diphenyl-1-picrylhydrazyl (DPPH) assay, and alkylation experiments suggested that cysteine residues contribute importantly to this activity. Dithio-bis-nitrobenzoic acid (DTNB)-based thiol quantification further demonstrated that rMfp6-1 contained abundant accessible free sulfhydryl groups, supporting an important contribution of cysteine-derived thiols to its antioxidant activity. Experiments on a full-thickness mouse wound model showed that rMfp6-1 treatment resulted in significantly faster wound contraction. Morphological analysis further revealed that rMfp6-1 optimizes the healing microenvironment by promoting collagen accumulation and re-epithelialization. Additionally, the treatment was found to trigger vascular endothelial growth factor (VEGF)-mediated angiogenesis, thereby improving the overall quality of the regenerated tissue. Furthermore, rMfp6-1 treatment significantly reduced interleukin-6 (IL-6) expression, suggesting that its antioxidant capacity creates a permissive microenvironment for tissue regeneration by suppressing excessive inflammation. These findings indicate that recombinant rMfp6-1 is a promising bioactive candidate for wound-healing applications. - Source: PubMed
Publication date: 2026/04/29
Li Zi-JunWang Kun-ChengShen Zhi-MingWang Yu-QingLi Yi-Feng - Covalent Fragment-Based Drug Discovery (FBDD) has emerged as a powerful strategy for unlocking challenging pharmacological targets and engaging shallow or "cryptic" binding pockets. In this study, we present the design and characterization of the Second Generation Covalent Fragment Library (CovLib Gen2), an expanded collection of 81 structurally diverse electrophiles tailored for Covalent Fragment-Based Drug Discovery (FBDD) using an electrophile-first approach. The library spans five distinct warhead classes, including epoxides, vinyl sulfones, acrylamides, α-cyanoacrylamides, and a core set of SɴAr-reactive heteroarenes. - Source: PubMed
Publication date: 2026/05/18
Schwer MartinAldea Sven REngelhardt Marc UStahlecker JasonRheinganz JanoschLangkamp AaronBoeckler Frank M - Understanding interfacial interactions at the native oxide surface of Mg is important for catalytic and biomedical applications. Recent advancements in plasmonic Mg research led to its use for surface-enhanced Raman scattering (SERS), a vibrational spectroscopy particularly sensitive to molecules bound to the enhancing substrate. Here, novel Mg film-over-nanospheres (FONs) are fabricated and used as SERS substrates to study molecular binding on Mg surfaces, augmenting previous results on 4-mercaptobenzoic acid (4-MBA) and 4-nitrothiophenol (4-NTP) by revealing the binding of 4-nitrophenol (4-NP) and 5,5'-dithiobis (2-nitrobenzoic acid) (DTNB). Through a systematic study of a total of 17 molecules with various functional groups, a p-related trend is unravelled: binding on natively oxidised Mg requires the adsorbate to dissociate and have a p between ∼4.5 and 7.5, however diselenides and ditellurides do not appear to follow this trend. The results pave the way for chemical functionalisation of Mg surfaces for plasmonic and other applications. - Source: PubMed
Publication date: 2026/04/29
Ten AndreyLomonosov VladimirPehlivan Zeki SemihRinge Emilie - Praziquantel (PZQ) is currently the only agent for treating schistosomiasis, but it is plagued by suboptimal efficacy to juvenile parasites, looming drug resistance, and inability to prevent reinfection. Thioredoxin glutathione reductase (TGR) is regarded as a promising therapeutic target due to its essential role in maintaining schistosome redox homeostasis. Herein, the crystal structures of Schistosoma japonicum TGR (SjTGR) in multiple redox states and in complex with NADPH, GSH, and the anti-helminthic agent Auranofin were elucidated. Structural analyses identified the hook-shaped conformation at the C-terminal redox center, which DTNB assays further confirmed enhances electron transfer efficiency. Structural and ITC data indicated that R317 was critical for NADPH binding via hydrogen-bond interactions. The analysis also indicated that the structure basis of Auranofin's potency was its tripartite interaction at the redox-active sites. In addition, we investigated the substrate specificity of SjTrx1i and SjTRP14, downstream proteins regulated by SjTGR, and elucidated the structural basis for this specificity by determining their oxidized/reduced structures. Furthermore, in vivo RNAi indicated knockdown of SjTGR or SjTRP14 blocked the survival and oviposition of schistosomes, thus ameliorating egg-induced granulomatous pathology in mice. This work provided a framework for knowledge-based design of novel anti-schistosomals targeting parasite-specific redox vulnerabilities. - Source: PubMed
Publication date: 2026/04/24
Wang SongqingHong WenbinZhong ShukunLiang ZhijianXiao TianyichenZhang ChuchuLiu XianshuDai ZiyiLi YunlongWu SiqiCai QixuWu CaimingHuang YuxuanHong PeichengRen HaixiaLi ShaoweiLin TianweiChen XueqinHuang Shuaiqin