Browse
Submit Data
Databases
API
Help

Dataset Information

15 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Protein-templated copper nanoclusters for fluorimetric determination of human serum albumin.

ABSTRACT: Copper nanoclusters (CuNCs) are attractive for their unique optical properties, providing sensitive fluorescent detection of several kinds of targets even in complex matrices. Their ability in growing on suitable protein and nucleic acid templates make CuNCs efficient optical reporters to be exploited in bioanalysis. In this work, we report the specific and sensitive determination of human serum albumin (HSA) in human serum (HS) and urine via CuNCs fluorescence. HSA is the most abundant protein in plasma, and plays a key role in the early diagnosis of serious pathological conditions such as albuminuria and albuminemia. Recently, HSA has become clinically central also as a biomarker to assess severity, progression, and prognosis of various cancers. We report the controlled and reproducible growth of CuNCs directly on the target analyte, HSA, which results in a fine dose-dependent fluorescent emission at 405 nm. The protocol is optimized in water, and then applied to serum and urine specimens, without matrix pretreatment. The method linearly responds within the whole concentration of clinical interest, with a sensitivity of 1.8 ± 0.1 × 10^-3 g L^-1 and 0.62 ± 0.03 × 10^-3 g L^-1 in serum and urine, respectively, and excellent reproducibility (CV_av% ca. 3% for both). The assay is designed to have a single protocol working for both matrices, with recovery of 95% (HS) and 96% (urine). The stability of the fluorescence after CuNCs formation was tested over 3 days, displaying good results (yet higher in urine than in serum).

SUBMITTER: Lettieri M

PROVIDER: S-EPMC7940276 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

pH-Regulated Synthesis of Trypsin-Templated Copper Nanoclusters with Blue and Yellow Fluorescent Emission.

Project description:In this article, a simple protocol to prepare water-soluble fluorescent copper nanoclusters (CuNCs) using trypsin as a stabilizer and hydrazine hydrate as a reducing agent was reported. It was found that the pH of the reaction solution was critical in determining the fluorescence of CuNCs. CuNCs with blue and yellow fluorescent emission were obtained under basic and acidic conditions, respectively. Although the detailed formation mechanisms of these CuNCs required further analysis, the synthetic route was promising for preparing different fluorescent metal NCs for applications. With good water solubility and excellent photostability, the yellow-emitting CuNCs could serve as a fluorescence probe for detection of Hg2+ based on the aggregation-induced quenching mechanism. The fluorescence quenching efficiency had fantastic linearity to Hg2+ concentrations in the range of 0.1-100 μM, with a limit of detection of 30 nM. Additionally, the yellow-emitting CuNCs exhibited negligible cytotoxicity and were successfully applied to bioimaging of HeLa cells.

| S-EPMC6045342 | biostudies-literature

Enhancing Liver Delivery of Gold Nanoclusters via Human Serum Albumin Encapsulation for Autoimmune Hepatitis Alleviation.

Project description:Peptide-protected gold nanoclusters (AuNCs), possessing exceptional biocompatibility and remarkable physicochemical properties, have demonstrated intrinsic pharmaceutical activity in immunomodulation, making them a highly attractive frontier in the field of nanomedicine exploration. Autoimmune hepatitis (AIH) is a serious autoimmune liver disease caused by the disruption of immune balance, for which effective treatment options are still lacking. In this study, we initially identified glutathione (GSH)-protected AuNCs as a promising nanodrug candidate for AIH alleviating in a Concanavalin A (Con A)-induced mice model. However, to enhance treatment efficiency, liver-targeted delivery needs to be improved. Therefore, human serum albumin (HSA)-encapsulated AuNCs were constructed to achieve enhanced liver targeting and more potent mitigation of Con A-induced elevations in plasma aspartate transaminase (AST), alanine transaminase (ALT), and liver injury in mice. In vivo and in vitro mechanism studies indicated that AuNCs could suppress the secretion of IFN-γ by Con A-stimulated T cells and subsequently inhibit the activation of the JAK2/STAT1 pathway and eventual hepatocyte apoptosis induced by IFN-γ. These actions ultimately protect the liver from immune cell infiltration and damage caused by Con A. These findings suggest that bio-protected AuNCs hold promise as nanodrugs for AIH therapy, with their liver targeting capabilities and therapeutic efficiency being further improved via rational surface ligand engineering.

| S-EPMC10818704 | biostudies-literature

Bovine serum albumin-templated nanoplatform for magnetic resonance imaging-guided chemodynamic therapy.

Project description:BackgroundNanotechnology in medicine has greatly expanded the therapeutic strategy that may be explored for cancer treatment by exploiting the specific tumor microenvironment such as mild acidity, high glutathione (GSH) concentration and overproduced hydrogen peroxide (H2O2). Among them, tumor microenvironment responsive chemodynamic therapy (CDT) utilized the Fenton or Fenton-like reaction to produce excess hydroxyl radical (·OH) for the destruction of tumor cells. However, the produced ·OH is easily depleted by the excess GSH in tumors, which would undoubtedly impair the CDT's efficiency. To overcome this obstacle and enhance the treatment efficiency, we design the nanoplatforms for magnetic resonance imaging (MRI)-guided CDT.ResultsIn this study, we applied the bovine serum albumin (BSA)-templated CuS:Gd nanoparticles (CuS:Gd NPs) for MRI-guided CDT. The Cu2+ in the CuS:Gd NPs could be reduced to Cu+ by GSH in tumors, which further reacted with H2O2 and triggered Fenton-like reaction to simultaneously generate abundant ·OH and deplete GSH for tumor enhanced CDT. Besides, the Gd3+ in CuS:Gd NPs endowed them with excellent MRI capability, which could be used to locate the tumor site and monitor the therapy process preliminarily.ConclusionsThe designed nanoplatforms offer a major step forward in CDT for effective treatment of tumors guided by MRI.

| S-EPMC6528315 | biostudies-literature

Improved Charge Transport across Bovine Serum Albumin–Au Nanoclusters’ Hybrid Molecular Junction

Project description:Proteins, a highly

| S-EPMC9219077 | biostudies-literature

Ultrafast hydration dynamics in protein unfolding: human serum albumin.

Project description:We report studies of unfolding and ultrafast hydration dynamics of the protein human serum albumin. Unique in this study is our ability to examine different domains of the same protein and the intermediate on the way to the unfolded state. With femtosecond resolution and site-selective labeling, we isolate the dynamics of domains I and II of the native protein, domain I of the intermediate at 2 M guanidine hydrochloride, and the unfolded state at 6 M of the denaturant. For studies of unfolding, we used the fluorophores, acrylodan (covalently bound to Cys-34 in domain I) and the intrinsic tryptophan (domain II), whereas for hydration dynamics, we probed acrylodan and prodan; the latter is bound to domain II. From the time-dependent spectra and the correlation functions, we obtained the time scale of dynamically ordered water: 57 ps for the more stable domain I and 32 ps for the less stable domain II, in contrast to approximately 0.8 ps for labile, bulk-type water. This trend suggests an increased hydrophilic residues-water interaction of domain I, contrary to some packing models. In the intermediate state, which is characterized by essentially intact domain I and unfolded domain II, the dynamics of ordered water around domain I is nearly the same (61 ps) as that of native state (57 ps), whereas that in the unfolded protein is much shorter (13 ps). We discuss the role of this fluidity in the correlation between stability and function of the protein.

| S-EPMC518771 | biostudies-literature

Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study.

Project description:Copper(II) complexes of thiosemicarbazones (TSCs) often exhibit anticancer properties, and their pharmacokinetic behavior can be affected by their interaction with blood transport proteins. Interaction of copper(II) complexes of an {N,N,S} donor α-N-pyridyl TSC (Triapine) and an {O,N,S} donor 2-hydroxybenzaldehyde TSC (STSC) with human serum albumin (HSA) was investigated by UV-visible and electron paramagnetic resonance spectroscopy at physiological pH. Asp-Ala-His-Lys and the monodentate N-methylimidazole were also applied as binding models. Conditional formation constants were determined for the ternary copper(II)-TSC complexes formed with HSA, DAHK, and N-methylimidazole based on the spectral changes of both charge transfer and d-d bands. The neutral N-methylimidazole displays a similar binding affinity to both TSC complexes. The partially negatively charged tetrapeptide binds stronger to the positively charged Triapine complex in comparison to the neutral STSC complex, while the opposite trend was observed for HSA, which demonstrates the limitations of the use of simple ligands to model the protein binding. The studied TSC complexes are able to bind to HSA in a fast process, and the conditional constants suggest that their binding strength is only weak-to-moderate.

| S-EPMC8125041 | biostudies-literature

Activation of Human Natural Killer Cells by Graphene Oxide-Templated Antibody Nanoclusters.

Project description:An emerging new paradigm is that immune cell activation is controlled by transient interactions between supramolecular assemblies of receptors and ligands. Current immunotherapy biologic pharmaceuticals that activate or desensitize NK cells are, however, individual molecules that do not replicate this nanoscale organization of proteins. Here, we use nanoscale graphene oxide (NGO) as a template to generate soluble nanoscale clusters of Natural Killer cell-activating antibodies. We control nanocluster size and molecular number to mimic reported values for cell surface proteins. These NGO-templated molecular nanoclusters, used to stimulate NK cells via the CD16 receptor, successfully induced cellular activation, indicated by degranulation of cytolytic granules and IFN-? secretion. Importantly, activation significantly exceeded that induced by the same antibodies applied as a solution of individual molecules. These results demonstrate that future immunotherapies could be enhanced by assembling immunomodulatory drugs into nanoclusters and establish NGO-templating as a candidate technology.

| S-EPMC5951604 | biostudies-literature

Stable Luminescent Poly(Allylaminehydrochloride)-Templated Copper Nanoclusters for Selectively Turn-Off Sensing of Deferasirox in β-Thalassemia Plasma.

Project description:Highly stable and facile one-pot copper nanoclusters (Cu NCs) coated with poly(allylamine hydrochloride) (PAH) have been synthesized for selectively sensing deferasirox (DFX) in β-thalassemia plasma. DFX is an important drug used for treating iron overloading in β-thalassemia, but needs to be monitored due to certain toxicity. In this study, the PAH-Cu NCs showed highly stable fluorescence with emission wavelengths at 450 nm. The DFX specifically interacted with the copper nanocluster to turn off the fluorescence of the PAH-Cu NCs, and could be selectively quantified through the fluorescence quenching effect. The linear range of DFX in plasma analyzed by PAH-Cu NCs was 1.0-100.0 µg/mL (r = 0.985). The relative standard deviation (RSD) and relative error (RE) were lower than 6.51% and 7.57%, respectively, showing excellent reproducibility of PAH-Cu NCs for sensing DFX in plasma. This method was also successfully applied for an analysis of three clinical plasma samples from β-thalassemia patients taking DFX. The data presented high similarity with that obtained through a capillary electrophoresis method. According to the results, the PAH-Cu NCs could be used as a tool for clinically sensing DFX in human plasma for clinical surveys.

| S-EPMC8706525 | biostudies-literature

Glutathione <i>S</i>-transferase templated copper nanoclusters as a fluorescent probe for turn-on sensing of chlorotetracycline.

Project description:Hereby, facile-green copper nanoclusters templated by glutathione S-transferase (GST-CuNCs) have been innovatively synthesized via a simple one-pot stirring method at room temperature. The as-prepared nanoclusters exhibited uniform size with satisfactory fluorescence intensity, good stability and low cytotoxicity. Significantly, the fluorescence of the obtained GST-CuNCs could be considerably enhanced by the addition of chlorotetracycline (CTC) rather than other analogues of CTC, which was ascribed to the aggregation-induced enhancement caused by the interaction between CTC and GST. The enhanced fluorescence intensity demonstrated a good linear correlation with the CTC concentration in the range of 30-120 μM (R2 = 0.99517), and the low detection limit was 69.7 nM. Furthermore, the proposed approach showed favorable selectivity and anti-interference toward CTC among prevalent ions and amino acids. Additionally, this nanoprobe was also applied to the quantitative detection of CTC in serum samples with satisfactory outcomes, which demonstrated excellent prospects for practical applications.

| S-EPMC10791131 | biostudies-literature

Human Serum Albumin Domain I Fusion Protein for Antibody Conjugation.

Project description:Bioorthogonal labeling of antibodies enables the conjugation of compounds, such as small molecules or peptides, which expand targeting capacity or enhance cytotoxicity. Taking advantage of a cyclohexene sulfonamide compound that site-selectively labels Lys64 in human serum albumin (HSA), we demonstrate that domain I of HSA can be used as a fusion protein for the preparation of antibody conjugates. Trastuzumab fusions were expressed at the N-terminus of the light chain or the C-terminus of the heavy chain enabling conjugation to small molecules. Moreover, these conjugates retained HER2 binding and proved to be highly stable in human plasma. Antibody conjugation via HSA domain I fusion should therefore have broad utility for making serum-stable antibody conjugates, particularly for antibody-drug conjugates.

| S-EPMC5367151 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data