scholarly journals How to Achieve High Encapsulation Efficiencies for Macromolecular and Sensitive APIs in Liposomes

Pharmaceutics ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 691
Author(s):  
Kirsten Ullmann ◽  
Gero Leneweit ◽  
Hermann Nirschl
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Encapsulation Efficiency ◽  
Active Pharmaceutical Ingredients ◽  
Pharmaceutical Ingredients ◽  
Bending Modulus ◽  
Vis Spectroscopy ◽  
The Stability ◽  
Very High

This research highlights the capacity of a newly introduced centrifugation process to form liposomes from water-in-fluorocarbon nano-emulsions stabilized with phospholipids to incorporate macromolecular and sensitive active pharmaceutical ingredients (API). The encapsulation efficiency of the produced liposomes, incorporating fluorescein-sodium, bovine serum albumin and fluorecein isothiocyanate dextran as model APIs, is determined by applying Vivaspin® centrifugation filtration and quantified by UV-Vis spectroscopy. It was found that higher densities of the fluorocarbons used as the hydrophobic phase enable a higher encapsulation efficiency and that an efficiency of up to 98% is possible depending on the used phospholipid. Among the engineering aspects of the process, a comparison between different membrane substances was performed. Efficiency increases with a higher phospholipid concentration but decreases with the addition of cholesterol. Due to the higher bending modulus, liposome formation is slowed down by cholesterol during liposome closure leading to a greater leakage of the model API. The encapsulation of bovine serum albumin and dextran, both investigated under different osmotic conditions, shows that an efflux negatively affects the encapsulation efficiency while an influx increases the stability. Overall, the process shows the potential for a very high encapsulation efficiency for macromolecules and future pharmaceutical applications.

scholarly journals Effect of Moderate UVC Irradiation on Bovine Serum Albumin and Complex with Antimetabolite 5-Fluorouracil: Fluorescence Spectroscopic and Molecular Modelling Studies

2015 ◽  
Vol 2015 ◽  
pp. 1-12 ◽  
Author(s):  
Shanmugavel Chinnathambi ◽  
Subramani Karthikeyan ◽  
Devadasan Velmurugan ◽  
Nobutaka Hanagata ◽  
Prakasarao Aruna ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Molecular Modelling ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Time Resolved ◽  
Vis Spectroscopy ◽  
Molecular Modelling Studies ◽  
Modelling Studies ◽  
The Stability

The interaction of antimetabolite 5-fluorouracil (5FU) with bovine serum albumin (BSA) under UVC (253.7 nm) irradiation was investigated in the present study using UV-Vis spectroscopy, steady state/time resolved fluorescence spectroscopic techniques. The stability of protein was found to be very strong when BSA gets bind to 5FU and moreover it is compared with the free BSA under UVC irradiation. From the fluorescence spectroscopic study, the stability of the complex was found to acquire 2-fold stronger than free protein. From the molecular modelling studies, we came to know the hydrogen bonds between BSA and antimetabolite 5FU are strong, up to 70.4 J/m2 under UVC irradiation.

Effect of the degree of glycation on the stability and aggregation of bovine serum albumin

2020 ◽  
Vol 106 ◽  
pp. 105892 ◽  
Author(s):  
Xuanting Liu ◽  
Jingbo Liu ◽  
Wenqi Zhang ◽  
Robin Pearce ◽  
Meiru Chen ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
The Stability

scholarly journals Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Materials ◽  
2021 ◽  
Vol 14 (2) ◽  
pp. 298
Author(s):  
Shufang Liu ◽  
Shu’e Wang ◽  
Zhanzuo Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Inner Filter Effect ◽  
Spectroscopic Techniques ◽  
Size Distributions ◽  
Size Dependent ◽  
Filter Effect ◽  
Vis Spectroscopy

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

Preparation and Application as Biosensor of Water-Soluble Conjugated Polyelectrolyte

2013 ◽  
Vol 538 ◽  
pp. 301-304
Author(s):  
Yi Ping Zhong ◽  
Rui Bin Hong ◽  
Bin Bin Yin ◽  
Ping Liu ◽  
Wen Ji Deng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Conjugated Polyelectrolyte ◽  
Sodium Sulfonate ◽  
Vis Spectroscopy

The water-soluble conjugated polyelectrolyte, poly[3-(1′-propyloxy-3′-sodium sulfonate) thiophene] (PTH-n3-SO3Na), was prepared. The interaction between the PTH-n3-SO3Na and bovine serum albumin (BSA) was investigated using UV-vis spectroscopy. It was found that the PTH-n3-SO3Na could be used as biosensor to detect BSA.

scholarly journals Ketoprofen-Based Ionic Liquids: Synthesis and Interactions with Bovine Serum Albumin

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 90 ◽  
Author(s):  
Paula Ossowicz ◽  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Joanna Klebeko ◽  
Ewelina Świątek ◽  
...  
Keyword(s):  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Binding Mode ◽  
Pharmaceutical Ingredients ◽  
System A ◽  
Static Mechanism

The development of ionic liquids based on active pharmaceutical ingredients (API-ILs) is a possible solution to some of the problems of solid and/or hydrophobic drugs such as low solubility and bioavailability, polymorphism and an alternative route of administration could be suggested as compared to the classical drug. Here, we report for the first time the synthesis and detailed characterization of a series of ILs containing a cation amino acid esters and anion ketoprofen (KETO-ILs). The affinity and the binding mode of the KETO-ILs to bovine serum albumin (BSA) were assessed using fluorescence spectroscopy. All compounds bind in a distance not longer than 6.14 nm to the BSA fluorophores. The estimated binding constants (KA) are in order of 105 L mol−1, which is indicative of strong drug or IL-BSA interactions. With respect to the ketoprofen-BSA system, a stronger affinity of the ILs containing l-LeuOEt, l-ValOBu, and l-ValOEt cation towards BSA is clearly seen. Fourier transformed infrared spectroscopy experiments have shown that all studied compounds induced a rearrangement of the protein molecule upon binding, which is consistent with the suggested static mechanism of BSA fluorescence quenching and formation of complexes between BSA and the drugs. All tested compounds were safe for macrophages.

Bovine Serum Albumin Nanoparticle Promotes the Stability of Quercetin in Simulated Intestinal Fluid

2011 ◽  
Vol 59 (11) ◽  
pp. 6292-6298 ◽  
Author(s):  
Ru Fang ◽  
Ruifang Hao ◽  
Xia Wu ◽  
Qi Li ◽  
Xiaojing Leng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Intestinal Fluid ◽  
Simulated Intestinal Fluid ◽  
The Stability

Activation and Inactivation of Phosphoenolpyruvate Carboxylase in Leaf Extracts From C4 Species

1978 ◽  
Vol 5 (5) ◽  
pp. 571 ◽  
Author(s):  
MD Hatch ◽  
IR Oliver
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphoenolpyruvate Carboxylase ◽  
Bovine Serum ◽  
Leaf Extracts ◽  
Small Molecular Weight ◽  
Carboxylase Activity ◽  
C4 Species ◽  
The Stability

The stability of phosphoenolpyruvate carboxylase (EC 4.1.1.31) was examined following extraction of the enzyme from leaves of several C4 plants. Extracts were rapidly processed on small Sephadex G-25 columns to free protein of small-molecular-weight compounds. With most of the species examined, activity was rapidly lost at both 0 and 25°C when the pH was about 7.8 or higher. Addition of bovine serum albumin to extracts incubated at 25°C and pH 8.2 not only prevented inactivation with several species, but resulted in a substantial increase in activity. The addition of dithiothreitol plus Mg2+ to extracts from some of these species reduced or prevented inactivation. With extracts maintained at 0°C, addition of either bovine serum albumin or dithiothreitol was effective only in reducing the rate of inactivation in extracts. Phosphoenolpyruvate carboxylase activity remained stable, or increased substantially, when extracts buffered between pH 7.4 and 6.9 were incubated at either 0 or 25°C. Activation was usually complete within an hour and was often significantly greater at 25°C or when bovine serum albumin was added. The activity of partially purified phosphoenolpyruvate carboxylase from Zea mays was similarly affected by pH, temperature, and bovine serum albumin. The present studies raise doubts about the accuracy of phosphoenolpyruvate carboxylase determinations made during the course of some previous studies on C4 species. Reliable procedures for the determination of phosphoenolpyruvate carboxylase activity in C4 plant extracts are described. Possible physiological implications of the results are considered.

scholarly journals Biogenic Ferrihydrite Nanoparticles Produced by Klebsiella oxytoca: Characterization, Physicochemical Properties and Bovine Serum Albumin Interactions

Nanomaterials ◽  
2022 ◽  
Vol 12 (2) ◽  
pp. 249
Author(s):  
Nicoleta Cazacu ◽  
Claudia G. Chilom ◽  
Sorina Iftimie ◽  
Maria Bălășoiu ◽  
Valentina P. Ladygina ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Denaturation ◽  
Klebsiella Oxytoca ◽  
Resonance Energy ◽  
Elemental Content ◽  
X Ray ◽  
Synthesis Of Nanoparticles ◽  
Vis Spectroscopy

The synthesis of nanoparticles inside microorganisms is an economical alternative to chemical and physical methods of nanoparticle synthesis. In this study, ferrihydrite nanoparticles synthesized by Klebsiella oxytoca bacterium in special conditions were characterized by scanning electron microscopy (SEM), energy-dispersive X-ray analysis (EDS), small-angle X-ray (SAXS), UV-Vis spectroscopy, fluorescence, fluorescence resonance energy transfer (FRET), and molecular docking. The morphology and the structure of the particles were characterized by means of SEM and SAXS. The elemental content was determined by means of the EDS method. The absorption properties of the ferrihydrite nanoparticles were investigated by UV-Vis spectroscopy. The binding mechanism of the biogenic ferrihydrite nanoparticles to Bovine Serum Albumin (BSA) protein, studied by fluorescence, showed a static and weak process, combined with FRET. Protein denaturation by temperature and urea in the presence of the ferrihydrite nanoparticles demonstrated their influence on the unfolding process. The AutoDock Vina and UCSF Chimera programs were used to predict the optimal binding site of the ferrihydrite to BSA and to find the location of the hydrophobic cavities in the sub-domain IIA of the BSA structure.

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