Study of Adsorption Behavior of Bilirubin on Human-Albumin Monolayer Using a Quartz Crystal Microbalance

Si, Shihui; Li, Si; Feng-lian, Ren; Zhu, Ding; Fung, YS

doi:10.1006/jcis.2002.8491

Cited by 30 publications

(15 citation statements)

References 24 publications

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“…(5)) [2]. Because free BR is present in a small amount relative to the albumin-BR complex, the concentration of the latter is almost equal to that of the unconjugated BR.…”

Section: Measurements In the Presence Of Albuminmentioning

confidence: 94%

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Superior sensing performance of multi-walled carbon nanotube-based electrodes to detect unconjugated bilirubin

et al. 2013

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The direct electrochemical behaviour of bilirubin in the physio-pathological concentration range and at physiological pH was investigated by cyclic voltammetry. Nanostructured electrodes with a thin film of multi-walled carbon nanotubes exhibited a higher sensing performance than bare electrodes. The detection limit obtained with nanostructured electrodes (4.2 ± 0.1 μM) allows the detection of both normal and pathological levels of bilirubin. Due to its sparse solubility in aqueous solvents, in human fluids bilirubin is found in the form of soluble complex with albumin. Therefore, the nanostructured-sensor response was studied in presence of different concentrations of this protein. A signal weakening was observed with increasing concentrations of albumin due to the decrease of free bilirubin. Finally, bilirubin detection was tested at concentrations typical of newborn jaundice (200-500 μM) and in the presence of normal albumin levels. A detection limit of 9.4 ± 0.3 μM was identified. Since this value is below the minimum critical bilirubin concentration for newborns, our sensor, modified with a thin film of carbon nanotubes, could potentially be used for bilirubin detection in cases of newborn jaundice.

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“…(5)) [2]. Because free BR is present in a small amount relative to the albumin-BR complex, the concentration of the latter is almost equal to that of the unconjugated BR.…”

Section: Measurements In the Presence Of Albuminmentioning

confidence: 94%

“…Conjugated BR forms a complex with gluconic acid, which renders it water soluble. Unconjugated BR, instead, tends to bind to albumin [2]. Therefore, the amount of free unconjugated BR in serum depends on the concentration of albumin and on the intrinsic ability of albumin to bind BR.…”

Section: Introductionmentioning

confidence: 99%

Superior sensing performance of multi-walled carbon nanotube-based electrodes to detect unconjugated bilirubin

et al. 2013

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“…Both procedures for protein immobilization were similar for all the substrates and they have been described elsewhere in detail [10,11,17]. The schematic diagram for them is presented in Fig.…”

Section: Protein Immobilizationmentioning

confidence: 99%

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

et al. 2007

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Two analytical methods, atomic force microscopy and quartz crystal microbalance, were applied to the study of the reaction kinetics occurring between concanavalin A and carboxypeptidase Y, presenting the specific lectin-carbohydrate recognition. The dissociation rate constants for concanavalin A-carboxypeptidase Y complex obtained using both atomic force microscopy and quartz crystal microbalance were of the same order of magnitude: k diss = 0.170 ± 0.060 s −1 and k diss = 0.095 ± 0.002 s −1 , respectively. In addition, each method alone aided in determining other parameters characterizing the studied interaction. Quartz crystal microbalance permitted us to estimate the association rate (k ass = (5.6 ± 0.1) × 10 4 M −1 s −1 ) and the equilibrium (Ka = (0.59 ± 0.01) × 10 6 M −1 ) constants for the binding process occurring between concanavalin A and mannose residues of carboxypeptidase Y under given experimental conditions. Atomic force microscopy in force spectroscopy mode enabled the determination of the energy barrier position of r = 2.29 ± 0.04Å characterizing the dissociation of concanavalin Acarboxypeptidase Y molecular complex. The presented results show that both atomic force microscopy and quartz crystal microbalance can be used to determine quantitative parameters characterizing the specific molecular interaction. Both methods can be easily combined for complementary and/or alternative studies of a chosen molecular interaction. By preparing the samples in the same manner the direct comparison between the data obtained via atomic force microscopy and quartz crystal microbalance can be made.

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“…Moreover, it is also possible to evaluate the kinetic profile of protein adsorption and associated conformational change on various surfaces (Shen et al, 2001). There have also been reports on using QCM-D for the investigation of adsorption/ desorption cycles (Si et al, 2002), protein subunits and peptides screening (Melles et al, 2005), density analysis of proteins (Voros, 2004) as well as solvent and ions influence on protein-protein interactions (Sadik and Cheung, 2001).…”

Section: Introductionmentioning

confidence: 98%

Quartz crystal microbalance with dissipation and microscale thermophoresis as tools for investigation of protein complex formation between thymidylate synthesis cycle enzymes

Antosiewicz

Senkara

Cieśla

2015

Biosensors and Bioelectronics

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Study of Adsorption Behavior of Bilirubin on Human-Albumin Monolayer Using a Quartz Crystal Microbalance

Cited by 30 publications

References 24 publications

Superior sensing performance of multi-walled carbon nanotube-based electrodes to detect unconjugated bilirubin

Superior sensing performance of multi-walled carbon nanotube-based electrodes to detect unconjugated bilirubin

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

Quartz crystal microbalance with dissipation and microscale thermophoresis as tools for investigation of protein complex formation between thymidylate synthesis cycle enzymes

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