Bovine Serum Albumin Modified Mg-Al Layered Double Oxides Nanohybrids: Preparation and Potential Application as Drug Carrier

2011 ◽  
Vol 396-398 ◽  
pp. 330-335
Author(s):  
Ting Fan ◽  
Hui Zhang ◽  
Shao Huan Guo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Physicochemical Properties ◽  
Bovine Serum ◽  
Drug Carrier ◽  
Double Oxide ◽  
Adsorption Behaviors ◽  
Structure Morphology ◽  
Model Protein ◽  
Ft Ir

Biocompatible MgAl-CO3-LDH-derived layered double oxide (LDO) as the host and bovine serum albumin (BSA) as a model protein have been chosen to fabricate a novel bioinorganic nanohybrid (BSA-LDO). The structure, morphology and physicochemical properties of the obtained nanohybrids are investigated by XRD, FT-IR, SEM and UV-vis methods and the interaction between LDO and BSA molecules has been discussed. The application of these nanohybrids as drug carrier is primarily studied by examining the adsorption behaviors of three drugs.

scholarly journals Isotachophoresis-based sample preparation of cellulases in sugarcane juice using bovine serum albumin as a model protein

2010 ◽  
Vol 1217 (51) ◽  
pp. 8026-8031 ◽  
Author(s):  
Ruchi Gupta ◽  
Sara J. Baldock ◽  
Peter R. Fielden ◽  
Jeff E. Prest ◽  
Bruce D. Grieve
Keyword(s):  
Bovine Serum Albumin ◽  
Sample Preparation ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sugarcane Juice ◽  
Model Protein

scholarly journals Studies on Thermal Aggregation of Bovine Serum Albumin as a Drug Carrier.

2000 ◽  
Vol 48 (4) ◽  
pp. 464-466 ◽  
Author(s):  
Chikako HONDA ◽  
Hiroko KAMIZONO ◽  
Tomomi SAMEJIMA ◽  
Kazutoyo ENDO
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Drug Carrier ◽  
Thermal Aggregation

scholarly journals Efficacy of Alcohol/sugar Aqueous Biphasic System on Partition of Bovine Serum Albumin

2020 ◽  
Author(s):  
Yin Hui Chow ◽  
Alagan Sahlini ◽  
Hui-Suan Ng ◽  
Chi-Wei Lan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Phase 1 ◽  
Biphasic System ◽  
Bottom Phase ◽  
Aqueous Biphasic System ◽  
Model Protein ◽  
Aqueous Biphasic ◽  
The Fourier Transform

Abstract A green bio-separation alternative can be performed with a non-toxic and biodegradable aqueous biphasic system (ABS) composed of short-chain aliphatic alcohol-based top phase (1-propanol and 2-propanol) and carbohydrate-based bottom phase (glucose, sucrose, and maltose). A model protein, bovine serum albumin (BSA) was adopted to determine the effects of types and concentration of phase-forming components; protein concentration; and system pH on the protein partition efficiency in the ABS. Results showed that the 1-propanol/maltose ABS gave an overall better partition efficiency of BSA to the alcohol-rich top phase compared to the 1-propanol/sucrose ABS, 1-propanol/glucose ABS, and 2-propanol/sugar ABS attributed to the lower hydrophilicity of 1-propanol and the stronger sugaring-out effect exerted by the maltose. A maximum partition coefficient (K) of 20.01 ± 0.05 and recovery yield (Y) of 95.42% ± 0.01 of BSA were obtained with the 35% (w/w) 1-propanol/22% (w/w) maltose ABS at pH 5.0 which contained 10% (w/w) BSA. The K and Y of BSA in 1-propanol/maltose ABS was further enhanced with the addition of 3% (w/w) of ionic liquids, 1-butyl-3-methylimidazolium bromide ([Bmim]Br) as the adjuvants which provides the protein stabilizing effect. The Fourier Transform Infrared Spectrum (FTIR) analysis revealed that the protein structure remained unaltered upon the separation process.

scholarly journals Formation of Nanocomplexes between Carboxymethyl Inulin and Bovine Serum Albumin via pH-Induced Electrostatic Interaction

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3056 ◽  
Author(s):  
Guiying Huang ◽  
Jun Liu ◽  
Weiping Jin ◽  
Zihao Wei ◽  
Chi-Tang Ho ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Electrostatic Interaction ◽  
Bovine Serum ◽  
Titration Calorimetry ◽  
Food Ingredients ◽  
Enthalpy Changes ◽  
Ft Ir

As a functional polysaccharide, inulin was carboxymethylated and it formed nanocomplexes with bovine serum albumin (BSA). The success of obtaining carboxymethyl inulin (CMI) was confirmed by a combination of Fourier transform Infrared (FT-IR), Raman spectroscopy, gel permeation chromatography (GPC), and titration. The effects of pH and ionic strength on the formation of CMI/BSA nanocomplexes were investigated. Our results showed that the formation of complex coacervate (pHφ1) and dissolution of CMI/BSA insoluble complexes (pHφ2) appeared in pH near 4.85 and 2.00 respectively. FT-IR and Raman data confirmed the existence of electrostatic interaction and hydrogen bonding between CMI and BSA. The isothermal titration calorimetry (ITC) results suggested that the process of complex formation was spontaneous and exothermic. The complexation was dominated by enthalpy changes (∆Η < 0, ∆S < 0) at pH 4.00, while it was contributed by enthalpic and entropic changes (∆Η < 0, ∆S > 0) at pH 2.60. Irregularly shaped insoluble complexes and globular soluble nanocomplexes (about 150 nm) were observed in CMI/BSA complexes at pH 4.00 and 2.60 while using optical microscopy and atomic force microscopy, respectively. The sodium chloride suppression effect on CMI/BSA complexes was confirmed by the decrease of incipient pH for soluble complex formation (or pHc) and pHφ1 under different sodium chloride concentrations. This research presents a new functional system with the potential for delivering bioactive food ingredients.

Bovine serum albumin adsorption on passivated porous silicon layers

2004 ◽  
Vol 82 (10) ◽  
pp. 1545-1553 ◽  
Author(s):  
L Tay ◽  
N L Rowell ◽  
D Poitras ◽  
J W Fraser ◽  
D J Lockwood ◽  
...  
Keyword(s):  
Porous Silicon ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Crystalline Silicon ◽  
Electrochemical Anodization ◽  
Undecylenic Acid ◽  
Ft Ir ◽  
Lift Off ◽  
Bsa Adsorption

Hydrogen-terminated porous silicon (pSi-H) films were fabricated through electrochemical anodization of crystalline silicon in hydrofluoric-acid-based solutions. The pSi-H surface was chemically functionalized by thermal reaction with undecylenic acid to produce an organic monolayer covalently attached to the silicon surface through Si—C bonds and bearing an acid terminal group. Bovine serum albumin (BSA) was adsorbed onto such surface-modified pSi structures. The resulting surfaces were characterized using scanning electron microscopy (SEM), reflection FT-IR spectroscopy, and ellipsometry. SEM showed that the porous films were damaged and partially lifted off the silicon substrate after a prolonged BSA adsorption. Ellipsometry analysis revealed that the BSA penetrated ∼1.3 µm into the porous structure. The film damage is likely a result of BSA anchoring itself tightly through strong electrostatic interaction with the acid-covered Si sidewalls. A change in surface tension during BSA film formation then causes the pSi layer to buckle and lift off the underlying Si substrate. FT-IR results from the undecylenic-acid-modified pSi surfaces before and after BSA adsorption showed the presence of strong characteristic amide I, II, and III vibrational bands after BSA adsorption. The surface properties of the pSi matrix and its interactions with BSA are examined in this study.Key words: ellipsometry, porous silicon, protein adsorption, surface passivation.

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