Human Albumin Research Articles (Page 1)

ABSTRACT Background Human albumin (HA) infusion may be effective for improving hypervolemic hyponatremia in cirrhosis. However, it remains unclear about whether HA dosage can influence its efficacy. Methods Overall, 288 cirrhotic patients with ascites and hypervolemic hyponatremia were retrospectively included and divided into high-dosage ( > 80 g) and low-dosage (≤80 g) HA groups during the period from first hyponatremia diagnosis to last HA infusion. Multivariate logistic regression analyses were performed to explore the impact of HA dosage on hyponatremia and serum albumin (ALB) level, and evaluate the impact of improvement of ALB on hyponatremia. Subgroup analyses were performed according to the baseline serum ALB level. Results High-dosage HA was independently associated with normalization of hyponatremia (OR = 1.919, p = 0.040) and improvement of ALB (OR = 3.001, p < 0.001). The effect of high-dosage HA on normalization of hyponatremia (OR = 2.108, p = 0.028) and improvement of ALB (OR = 2.926, p = 0.001) remained significant in patients with a baseline ALB level of < 30 g/L. Improvement of ALB was independently associated with normalization of hyponatremia (OR = 2.108, p = 0.014). The effect remained significant in patients with a baseline ALB level of < 30 g/L (OR = 2.228, p = 0.019). Conclusions High-dosage HA should be superior to low-dosage HA for correcting hypervolemic hyponatremia in cirrhosis, especially in those with a baseline ALB level of < 30 g/L, probably due to its significant benefit in the improvement of ALB.

Kidney and liver disorders pose significant health challenges in companion animals. Human serum albumin (HSA) has been identified as a promising biomarker for these conditions in humans. Given the high sequence similarity (∼80%) among HSA, canine (CSA), and feline (FSA) serum albumins, this study investigates the feasibility of using CSA and FSA as biomarkers for kidney dysfunction in veterinary diagnostics. Graphene-based aptasensors have shown promise for selective albumin detection. Graphene acts as a sorbent for fluorescent dye-labeled HSA-selective aptamer. The HSA concentration is determined by the recovery of the fluorescence intensity. With a comparable size to aptamers, noncytotoxicity, and high biocompatibility of graphene quantum dot (GQD), it is attractive to explore the use of aptamer-functionalized GQD (GQDA) to recognize pet albumins. Herein, Molecular Dynamics (MD) simulations were performed to evaluate the binding of GQDA to CSA and FSA in comparison to HSA. The results indicate the spontaneous GQDA-albumin complex. Lysines and arginines serve as the main contributors. CSA binds GQDA through domain III like HSA, where the aptamer 3' tail serves as a key recognition site. In contrast, FSA shows weak binding to GQDA. FSA interacts with a rigid hairpin loop at the aptamer 5' end, which limits its accessibility. Overall, our findings suggest that the HSA-selective GQDA complex has strong potential to recognize CSA, but not FSA. This insight supports the future design of diagnostic tools for detecting kidney and liver dysfunction in canine patients.

Human serum albumin (HSA) has three major binding sites for drugs: Site I, Site II, and FA1 site. Dansyl amino acids (Dans-AAs) have long been used as convenient markers to judge whether a low molecular weight molecule of interest (ligand) binds to Sites I or II. However, crystal structures of HSA-Dans-AA complexes have revealed that Dans-AAs with strict site specificity are also bound to non-marker sites. To characterize the multiple binding of Dans-AAs in detail, the average number of the bound ligands per HSA molecule were obtained in a free ligand concentration of 1-400μM for dansylate (DA) and 17 Dans-AAs using microbore frontal gel filtration chromatography. Analysis of the binding curves indicated that there are three specific binding sites for Dans-AAs. Four Dans-AAs with hydrophobic sidechain bind to all the sites with identical affinity, whereas DA and four Dans-AAs bind equally to two of them. Nine Dans-AAs bind to one of the three sites with the maximum occupancy ranging from 72 to 94%. The UV-vis absorption spectrum of HSA-ligand complex was obtained for DA and 10 Dans-AAs, revealing that the dansyl moiety is in hydrophobic environment and conformational changes in the binding site residues are induced.

Accurate and multiplexed detection of protein biomarkers in complex biological fluids is essential for early diagnosis and precision medicine. However, existing technologies face critical trade-offs among sensitivity, specificity, multiplexing capability, and operational simplicity. Antibody-based assays like ELISA often lack the sensitivity for early detection, while nucleic acid amplification methods are poorly suited for protein targets and require complex workflows. This creates a pressing need for a simple, highly sensitive, and interference-free approach for simultaneous protein detection in real-world samples. Here, we report an aptamer-driven T7 RNA polymerase cascade amplification system for visual, dual-channel detection of protein biomarkers directly in serum. The platform converts target recognition into isothermal RNA transcription, producing red or green fluorescence via fluorogenic RNA-dye complexes. Using alpha-fetoprotein and human serum albumin as models, the system achieved femtogram-per-milliliter sensitivity, excellent specificity, and broad linear ranges. A red-green fluorescence logic enables intuitive clinical interpretation. Validation with spiked and clinical samples showed recovery rates between 90 and 110% and strong agreement with ELISA results. These findings demonstrate that protein-responsive nucleic acid circuits can achieve precise, multiplexed detection with instrument-free signal amplification. By integrating molecular recognition, signal amplification, and visual readout, this strategy offers a scalable, point-of-care diagnostic framework and contributes to advancing protein-regulated synthetic biology circuits.

The global prevalence of diabetes is rising at an alarming rate, making it the third leading cause of death worldwide. This study presented a user-friendly, straightforward, and non-invasive method for screening diabetes. Various antibody-conjugated boronic acid-modified gold nanoparticles (Ab-AuNPs) were prepared, including anti-HbA1c, anti-HBA1, anti-HSA, anti-gHSA, and anti-insulin, to enable the specific recognition of their corresponding antigens in single droplet samples of urine and saliva on nitrocellulose membranes, with subsequent analysis performed using laser desorption/ionization mass spectrometry (LDI-MS). Ab-AuNPs absorbed ultraviolet laser light, leading to the direct desorption and ionization of Au ions. This process eliminated the need for an additional organic matrix in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), effectively reduced interference from matrix-related ions, and significantly amplified the detection signal of Au ions at trace levels for targeted antigens in urine and saliva. The developed method revealed elevated levels of glycated proteins, including glycated hemoglobin (HbA1c) and glycated human serum albumin (gHSA), as well as human serum albumin (HSA), in diabetic patients compared to healthy individuals. In contrast, insulin levels were notably lower in diabetic patients. By analyzing these biomarker changes, we successfully identified the presence of diabetes. The reported method for screening diabetes in biological fluids provides a practical approach and holds significant promise for analyzing other diseases as corresponding biomarkers are discovered and their antibodies are developed and acquired in the future.

BackgroundThe aim of this study is to evaluate whether the use of Oxygen Reserve Index (ORi) can prevent hyperoxia in patients undergoing rhinoplasty surgery and whether it can reduce oxidative stress caused by hyperoxia.MethodsA total of 60 patients, who were scheduled for rhinoplasty surgery and had an American Society of Anesthesiologists (ASA) score of I and II, were included in the study. The patients were randomly divided into two groups: the ORi group (Group R) and the control group (Group C). In Group R, oxygen support was titrated to keep the ORi values close to zero. In the control group, oxygen support was provided conventionally. Arterial blood gas samples were taken after intubation, at the 120th minute of the surgery and at the end of the surgery to record partial arterial oxygen pressure (PaO₂) values. During this process, patients’ peripheral oxygen saturation (SpO₂) and ORi values were continuously recorded along with hemodynamic data. Preoperative and postoperative blood samples were collected from both groups, and oxidative stress was assessed by evaluating thiol-disulfide homeostasis and ischemia-modified albumin (IMA), which are current indicators of oxidative stress.ResultsThe demographic characteristics and the surgical durations were similar between the groups. PaO₂ values were lower in Group R compared to Group C. ORi values were correlated with PaO₂ values. Preoperative native thiol, total thiol, and disulfide values were similar in both groups. In both groups, postoperative native thiol, total thiol, and disulfide values decreased compared to the preoperative period, while IMA values increased. In Group R, the decrease in native thiol and total thiol values and the increase in IMA values were less than in Group C.ConclusionWe concluded that ORi guided oxygen titration may reduce the severity of hyperoxia and may decrease oxidative stress in rhinoplasty surgery.Trial registrationClinicalTrials.gov Identifier NCT07158073. Registered on 21 August 2025.Supplementary InformationThe online version contains supplementary material available at 10.1186/s12871-025-03424-0.

Human serum albumin (HSA), the most abundant plasma protein predominantly synthesized and secreted by the liver, harbors atypical N-glycosylation modifications at Asn68 and Asn123. Despite their potential biological relevance, the comprehensive characterization of these modifications remains limited. Here, we systematically characterized atypical N-glycosylation on HSA using a sialic acid linkage-specific derivatization strategy coupled with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS), identifying 35 N-glycans including 23 sialylated N-glycans distinguished sialic acid linkage isomers. LC-ESI-MS analysis further resolved 25 site-specific N-glycopeptides, establishing the most detailed HSA N-glycosylation profile to date and elucidating its structural diversity. Given the liver-specific origin of HSA, we further explored the clinical relevance of HSA glycosylation in serum samples from healthy controls (HC), liver cirrhosis (LC), and hepatocellular carcinoma (HCC) patients and found that HSA glycopeptides exhibited exceptional diagnostic accuracy in distinguishing LC from HCC patients (AUC = 0.906). These findings not only decode the complexity of HSA glycosylation but also validate its clinical utility as a liver-specific biomarker for HCC detection.

Pregnenolone-carbamate derivatives were synthesized and evaluated as potential multifunctional agents with cholinesterase inhibitory and neuroprotective properties. Among them, P3, P5, and P9 exhibited the most promising profiles and were subjected to integrated spectroscopic, biochemical, and computational analyses. Inhibition assays revealed selective acetylcholinesterase (AChE) inhibition by P3 (IC50 = 0.11 μM), butyrylcholinesterase inhibition (BuChE) selectivity for P5 (IC50 = 0.47 μM), and dual inhibition by P9. Fluorescence and UV-vis studies indicated minor groove binding to DNA with log Kapp values around 5.85, while static quenching with human serum albumin (HSA) was observed, with log KA values up to 2.25. Docking studies supported these findings, showing favorable binding energies for DNA (-8.6 kcal/mol) and HSA (-9.7 kcal/mol), and predicted localization within the DNA minor groove and Sudlow sites on HSA. Cytotoxicity assays on HT22 cells indicated high viability (> 75% at 40 µM), suggesting a favorable safety margin. These results offer a molecular-level understanding of the pharmacodynamic and pharmacokinetic properties of these compounds and support their potential for further in vivo evaluation.

Resolving SPARC-HSA binding kinetics with an ultrasensitive photonic sensor based on bound states in the continuum.

Human serum albumin-adduct biomarkers to prove human poisoning with methanethiol.

Size-adjustable nanoparticles co-target macrophages and endothelial cells for enhanced atherosclerosis therapy.

Click conjugation of trivalent mannosyl glycocluster with human serum albumin to generate a cell targeting delivery vehicle.

Interaction of novel betaine-PEG deep eutectic solvents with bovine and human serum albumin: protein structure modulation and antioxidant activity

Exploring the binding interactions of flufenoxuron and hexaflumuron with human serum albumin: experimental and computational perspectives

Role of folate functionalized human serum albumin nano-formulation for bleomycin delivery on gene expression in gastric cancer cells.

GSH-activable and cytolytic iPep-coupled immune nanoagonist for cancer synergetic therapy.

Molecular insights into the binding of human serum albumin to charged dendritic nanomicelles: A synergistic experimental and in silico approach

Tianeptine: enantiomeric separations, structural assignment, and biological interactions.

A novel peptide excipient stabilizes DaxibotulinumtoxinA.

Oxygen-boosted nanodrug for amplified ferroptosis-photodynamic immunotherapy together with PD-1 checkpoint blockade against triple-negative breast cancer.