Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin

Maity, Arnab; Pal, Uttam; Chakraborty, Brotati; Sengupta, Chaitrali; Sau, Abhishek; Chakraborty, Swatadipta; Basu, Samita

doi:10.1016/j.ijbiomac.2019.06.126

Cited by 22 publications

(8 citation statements)

References 56 publications

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“…BSA as a typical protein model is widely investigated because of the similar amino sequence to human serum albumin [ 52 ]. It has been reported that BSA can be adsorbed on solid surfaces through a complex process, including van der Waals, hydrophobic, electrostatic interactions, and hydrogen bonds [ 53 ].…”

Section: Discussionmentioning

confidence: 99%

Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline

Liu

Lü

Zhang³

2021

J Mater Sci: Mater Med

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Zinc (Zn) and its alloys have received increasing attention as new alternative biodegradable metals. However, consensus has not been reached on the corrosion behaviour of Zn. As cardiovascular artery stent material, Zn is supposed to contact with plasma that contains inorganic salts and organic components. Protein is one of the most important constitute in the plasma and could adsorb on the material surface. In this paper, bovine serum albumin (BSA) was used as a typical protein. Influences of BSA on pure Zn corrosion in phosphate buffered saline is investigated as a function of BSA concentrations and immersion durations by electrochemical techniques and surface analysis. Results showed that pure Zn corrosion was progressively accelerated with BSA concentrations (ranging from 0.05 to 5 g L−1) at 0.5 h. With time evolves, formation of phosphates as corrosion product was delayed by BSA adsorption, especially at concentration of 2 g L−1. Within 48 h, the corrosion of pure Zn was alleviated by BSA at concentration of 0.1 g L−1, whereas the corrosion was enhanced after 168 h. Addition of 2 g L−1 BSA has opposite influence on the pure Zn corrosion. Furthermore, schematic corrosion behaviour at protein/Zn interfaces was proposed. This work encourages us to think more about the influence of protein on the material corrosion and helps us to better understand the corrosion behaviour of pure Zn.

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Section: Discussionmentioning

confidence: 99%

Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline

Liu

Lü

Zhang³

2021

J Mater Sci: Mater Med

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“…In contrast, the absorption study implied the formation of a ground-state complex between Ru:CNDEDAs and BSA/HSA. The transfer of energy from BSA/HSA to Ru:CNDEDAs was also demonstrated and the efficiency of this energy transfer was highly dependent on the stability of the protein nanoparticle complex (Maity et al 2019 ). In another study, dynamic quenching of protein fluorescence was observed and C-dots had no significant effect on HSA or γ-globulin structure.…”

Section: Plasma Proteinsmentioning

confidence: 99%

Application of non-metal nanoparticles, as a novel approach, for improving the stability of blood products: 2011–2021

Mehrizi

Ardestani

2022

Prog Biomater

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Despite the importance of the proper quality of blood products for safe transfusion, conventional methods for preparation and their preservation, they lack significant stability. Non-metal nanoparticles with particular features may overcome these challenges. This review study for the first time provided a comprehensive vision of the interaction of non-metal nanoparticles with each blood product (red blood cells, platelets and plasma proteins). The findings of this review on the most effective nanoparticle for improving the stability of RBCs indicate that graphene quantum dots and nanodiamonds show compatibility with RBCs. For increasing the stability of platelet products, silica nanoparticles exhibited a suppressive impact on platelet aggregation. Pristine graphene also shows compatibility with platelets. For better stability of plasma products, graphene oxide was indicated to preserve free human serum albumin from thermal shocks at low ionic strength. For increased stability of Factor VIII, mesoporous silica nanoparticles with large pores exhibit the superb quality of recovered proteins. Furthermore, 3.2 nm quantum dots exhibited anticoagulant effects. As the best promising nanoparticles for immunoglobulin stability, graphene quantum dots showed compatibility with γ-globulins. Overall, this review recommends further research on the mentioned nanoparticles as the most potential candidates for enhancing the stability and storage of blood components. Graphical abstract

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“…As no significant change occurred in the temperature, the enthalpy change (ΔH) was considered to be constant. The thermodynamic parameters ΔH, ΔG (energy change), and ΔS (entropy change) were obtained using the following equations [23] :…”

Section: Thermodynamic Parametersmentioning

confidence: 99%

“…However, the results of the in vitro blood coagulation showed that the SG-CCDs did not interfere with the coagulation process. The reason may have been that in the hFIB-SG-CCD system, the hFIB and SG-CCDs encountered collisions without complex formation, so the hFIB could rapidly reach a steady equilibrium conformation on the nano-SG-CCD surfaces [23] with no effects on the coagulation process.…”

Section: Effect Of Sg-ccds On In Vitro Blood Coagulationmentioning

confidence: 99%

Synthesis of cationic carbon dots and their effects on human serum proteins and in vitro blood coagulation

et al. 2021

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Cationic carbon dots (CCDs) are a promising alternative to gene-delivery systems, and good biosafety levels are crucial for their in vivo use. In this study, spherical and monodispersed CCDs with an average surface potential of +28.7 mV were prepared using sucrose and glutamate (denoted SG-CCDs) using a one-pot autoclave-assisted method. Molecular interactions between the SG-CCDs and four major human serum proteins (albumin, immunoglobulin G, fibrinogen, and transferrin) were investigated.The results were further verified on human serum, and the effect of the SG-CCDs on in vitro blood coagulation was examined. The results showed that the fluorescence of human serum was clearly quenched by the SG-CCDs through a dynamic collision mechanism. Moreover, SG-CCDs at a concentration of 20 μM exhibited minor effects on the secondary structure of human serum. The activated partial thromboplastin and prothrombin time as well as the fibrinogen concentration were not changed, indicating that the SG-CCDs did not interfere with the coagulation process. This study provided an understandable background on the behaviour of CCDs in clinical applications.

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Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin

Cited by 22 publications

References 56 publications

Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline

Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline

Application of non-metal nanoparticles, as a novel approach, for improving the stability of blood products: 2011–2021

Synthesis of cationic carbon dots and their effects on human serum proteins and in vitro blood coagulation

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