Development and validation of a high-performance liquid chromatography (HPLC) method for the determination of human serum albumin (HSA) in medical devices

Eertmans, Frank; Bogaert, Veerle; Puype, Barbara

doi:10.1039/c1ay05148b

Cited by 34 publications

(10 citation statements)

References 25 publications

(28 reference statements)

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“…Although each of the mentioned compounds has been extensively studied and information about them can be found in the literature [10][11][12][13][14][15], no method for the simultaneous determination of HSA and TM has been reported up to the present day.…”

mentioning

confidence: 99%

RP-HPLC method development for the simultaneous determination of timolol maleate and human serum albumin in albumin nanoparticles

Boiero

Allemandi

Longhi

et al. 2015

Journal of Pharmaceutical and Biomedical Analysis

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An isocratic high-performance liquid chromatographic method was developed and validated for the simultaneous determination of human serum albumin (HSA) and timolol in albumin nanoparticles. This method involved a reversed-phase-C18 column thermostated at 25 °C, UV detection at 276 nm, flow rate of 1.0 ml/min and a mobile phase compounded by 0.05% (v/v) trifluoroacetic acid in water/0.05% (v/v) trifluoroacetic acid in an acetonitrile (40:60, v/v) solution. The elution times for albumin and timolol were 1.84 ± 0.05 min and 2.67 ± 0.04 min, respectively. Calibration curves were linear from 0.2 to 100 mg/ml for HSA and 0.01 to 1 mg/ml for timolol. Limits of quantification were 0.2 mg/ml for HSA and 0.01 mg/ml for timolol. The values of accuracy and precision of intra- and inter-day variation studies were within acceptable limits, according to the US Food and Drug Administration Guidance for Industry. The described method has proved to be useful to give accurate measurements of human serum albumin and timolol from albumin nanoparticles to determine the percentage of encapsulation and the process yield.

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mentioning

confidence: 99%

RP-HPLC method development for the simultaneous determination of timolol maleate and human serum albumin in albumin nanoparticles

Boiero

Allemandi

Longhi

et al. 2015

Journal of Pharmaceutical and Biomedical Analysis

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“…The inset of Figure 3 B showed that the fluorescence intensity had a linear relationship (R 2 = 0.9976) with HSA concentration in the concentration range of 0.15–2.5 μM, and the regression equation was Y = −313.35 X + 1064.3, where Y was the fluorescence intensity at 610 nm and X was the HA concentration. The limit of detection (LOD) of the proposed strategy was estimated to be 0.082 μM, which was lower and more rapid than the other methods [ 38 , 39 , 40 ]. Therefore, a simple, rapid, effective and sensitive method of HA determination was established.…”

Section: Resultsmentioning

confidence: 93%

A Novel Detection Method of Human Serum Albumin Based on the Poly(Thymine)-Templated Copper Nanoparticles

Chen

Xiang

et al. 2017

Sensors

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In this work, we developed a facile fluorescence method for quantitative detection of human serum albumin (HSA) based on the inhibition of poly(thymine) (poly T)-templated copper nanoparticles (CuNPs) in the presence of HSA. Under normal circumstances, poly T-templated CuNPs can display strong fluorescence with excitation/emission peaks at 340/610 nm. However, in the presence of HSA, it will absorb cupric ion, which will prevent the formation of CuNPs. As a result, the fluorescence intensity will become obviously lower in the presence of HSA. The analyte HSA concentration had a proportional linear relationship with the fluorescence intensity of CuNPs. The detection limit for HSA was 8.2 × 10−8 mol·L−1. Furthermore, it was also successfully employed to determine HSA in biological samples. Thus, this method has potential applications in point-of-care medical diagnosis and biomedical research.

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“…[ 6 ] As seen in Figure 6, the formation of DNA‐protein contacts in both BSA and CSA mainly employ arginine (R) and lysine (K) where both residues were reported to be a key for the formation of DNA‐protein complex. [ 7–8 ] R‐DG, R‐DC, K‐DG, and K‐DT hydrogen bonds formed by side chains and nucleobase were illustrated as the first fourth most significant interactions in protein‐DNA complexes. [ 4 ] Thus comparing to CSA, a higher number of DNA base‐amino acid interactions in BSA is a result of a higher number of constant R‐DG, R‐DC, K‐DG, and K‐DT hydrogen bonds observed in BSA (Figure 5B and 6).…”

Section: Methodsmentioning

confidence: 99%

“…[4,5] Moreover, the amount of albumin can serve as a diagnostic marker malnutrition, infection, and inflammation. [3] A number of methods such as electrochemistry, [6] liquid chromatography, [7] surface Abbreviations: BSA, bovine serum albumin; CSA, canine serum albumin; HSA, human serum albumin; MD, molecular dynamics.…”

Section: Introductionmentioning

confidence: 99%

“…[ 4,5 ] Moreover, the amount of albumin can serve as a diagnostic marker malnutrition, infection, and inflammation. [ 3 ] A number of methods such as electrochemistry, [ 6 ] liquid chromatography, [ 7 ] surface enhanced Raman scattering [ 8 ] were employed for albumin count in both serum and urine, however these methods are limited to cost, response time, sensitivity, and a need of professional operator. Alternatively, fluorescent assay becomes one of most widely applied techniques for albumin measurement.…”

Section: Introductionmentioning

confidence: 99%

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How human serum albumin‐selective DNA aptamer binds to bovine and canine serum albumins

2021

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Serum albumin (SA) is the most abundant carrier protein in blood. SA carries a diverse range of nutrients, drugs, and metal ions. It has wide clinical and biochemical applications. Human serum albumin (HSA) can be used as a biomarker for kidney and liver diseases. Aptasensor is one of potential HSA detection methods. HSA-specific aptamer was selected for HSA detection. In animals, bovine serum albumin (BSA) and canine serum albumins (CSA) share high sequence similarities to HSA. Thus, it is interesting to explore the possibility of using HSA-selective aptamer for BSA and CSA aptasensor. In this study, molecular dynamics (MD) simulations were initially employed to investigate the binding of aptamer to BSA and CSA in comparison to HSA. Like HSA, both BSA and CSA can bind aptamer, but different binding affinities are observed. BSA shows the tighter binding to aptamer than CSA. Domain III is found to be the aptamer-binding domain although no specific aptamer conformation is captured. However, in all cases, the aptamer utilizes the 3 0-end to attach on an albumin surface. Both nucleobases and phosphate backbones on a DNA aptamer are important for albumin-aptamer complexation. Our results imply the possibility of using HSA-specific aptamer for BSA detection due to tighter binding observed, but may be less effective in CSA. However, the test in actual complicated condition must be further studied.

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Development and validation of a high-performance liquid chromatography (HPLC) method for the determination of human serum albumin (HSA) in medical devices

Cited by 34 publications

References 25 publications

RP-HPLC method development for the simultaneous determination of timolol maleate and human serum albumin in albumin nanoparticles

RP-HPLC method development for the simultaneous determination of timolol maleate and human serum albumin in albumin nanoparticles

A Novel Detection Method of Human Serum Albumin Based on the Poly(Thymine)-Templated Copper Nanoparticles

How human serum albumin‐selective DNA aptamer binds to bovine and canine serum albumins

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