scholarly journals Sintesis Nanopartikel Bovine Serum Albumin Kombinasi Cisplatin dan Asam Folat Sebagai Kandidat Antikanker

2020 ◽  
Vol 3 (2) ◽  
pp. 79
Author(s):  
Ersalina Nidianti ◽  
Ary Andini ◽  
Nia Kurniaty Rukman
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ft Ir

<p>Kanker adalah penyakit tidak menular yang menyebabkan morbiditas dan mortalitas di seluruh wilayah dunia. Salah satu pengobatan kanker adalah dengan menggunakan obat kemoterapi cisplatin. Namun cisplatin memiliki efek samping yang bersifat toksik jika dikonsumsi dalam dosis dan waktu tertentu. Kombinasi nanopartikel <em>bovine serum albumin </em>(BSA) yang mengandung cisplatin dikembangkan dengan modifikasi ikatan menggunakan asam folat sebagai solusi alternatif meminimalisir efek toksik yang dihasilkan dan mengoptimalkan sistem pengiriman obat. Tujuan penelitian adalah sintesis kombinasi nanopartikel BSA yang mengandung cisplatin dan modifikasi ikatan menggunakan asam folat sebagai kandidat antikanker. Penelitian ini dilakukan melalui sintesis dengan metode desolvasi. Hasil penelitian menunjukkan bahwa nanopartikel BSA yang dikombinasi dengan cisplatin dan asam folat telah berhasil disintesis. Analisis FT-IR menunjukkan bahwa ada gugus fungsi O-H alkohol, C-H, C-C, NO<sub>2</sub> yang berperan dalam sintesis nanopartikel. Analisis XRD menunjukkan adanya pergeseran <em>peak</em> dari NP-BSA 31,69 menjadi As-CP-NP-BSA 34,45; ukuran nanopartikel NP-BSA 2,38 nm dan As-CP-NP-BSA 2,62 nm sedangkan analisis SEM-EDX diketahui ada unsur C, O, Mg, Cl dan Pt.</p>

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.

scholarly journals Study on the interaction of Prodigiosin with bovine serum albumin by spectroscopic methods

2012 ◽  
Vol 27 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Shu-Chao Liu ◽  
Jing Tang ◽  
Xi-Hai Zhang ◽  
Yuan-Yuan Gao ◽  
Fei Ma ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Synchronous Fluorescence ◽  
Spectroscopic Methods ◽  
Amino Acid Residues ◽  
Absorption And Fluorescence Spectra ◽  
Ft Ir ◽  
Spectrum Experiment

The interaction between bovine serum albumin (BSA) and Prodigiosin (PG) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, FT-IR and circular dichroism (CD) techniques. The data of UV-vis absorption and fluorescence spectra displayed that there existed interaction between PG and aromatic amino acid residues of BSA. The synchronous fluorescence and CD spectrum experiment both showed that the secondary structure of BSA changed with addition of PG. All these results revealed that the conformation and microenvironment of BSA were changed.

FT-IR for the Soluble Complexes of Bovine Serum Albumin Reacted with Calcium Hydroxyapatites

1999 ◽  
Vol 15 (12) ◽  
pp. 1064-1069 ◽  
Author(s):  
Shen Yu-Hua ◽  
◽  
Yang Zhan-Lan ◽  
Wu Jin-Guang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ft Ir ◽  
Soluble Complexes

scholarly journals Adsorption of bovine serum albumin onto synthetic Fe-doped geomimetic chrysotile

2015 ◽  
Vol 12 (107) ◽  
pp. 20150186 ◽  
Author(s):  
Alessio Adamiano ◽  
Isidoro Giorgio Lesci ◽  
Daniele Fabbri ◽  
Norberto Roveri
Keyword(s):  
Gas Chromatography ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Health Hazard ◽  
Random Coil ◽  
Gas Chromatography Mass Spectrometry ◽  
Gravimetric Analysis ◽  
Minute Amount ◽  
Ft Ir

Synthetic stoichiometric and Fe-doped geomimetic chrysotile nanocrystals represent a reference standard to investigate the health hazard associated with mineral asbestos fibres. Experimental evidence suggests that the generation of reactive oxygen species and other radicals, catalysed by iron ions at the fibre surface, plays an important role in asbestos-induced cytotoxicity and genotoxicity. In this study, structural modification of bovine serum albumin (BSA) adsorbed onto synthetic chrysotile doped with different amounts of Fe has been investigated by Fourier transform infrared spectroscopy (FT-IR), thermal gravimetric analysis (TGA) and analytical pyrolysis coupled with gas chromatography–mass spectrometry. FT-IR data evidenced a marked increase in disordered structures like random coil and β-turn of BSA–nanocrystal adduct with 0.52 wt% of Fe doped. The TGA profile of the BSA revealed that its interaction with the synthetic chrysotile surface was strongly affected by the substitution of Fe into the chrysotile structure. The 2,5-diketopiperazine yields, formed upon thermal degradation of the polypeptide chain (pyrolysis–gas chromatography), changed when the BSA was adsorbed on the nanofibres. In general, results suggested that minute amount (less than 1 wt%) of Fe doping in chrysotile affected the protein–nanofibre interactions, supporting the role that this element may play in asbestos toxicity. The catalytic role of iron and the consequent unfolding of protein due to the structural surface modification of nanofibres were also evaluated.

scholarly journals Interaction of levothyroxine with bovine serum albumin: a spectroscopic assay

2020 ◽  
Author(s):  
Nicoleta Sandu ◽  
Claudia G. Chilom ◽  
Melinda David ◽  
Monica Florescu
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Vis Spectroscopy ◽  
Ft Ir ◽  
Exogenous Compounds

ABSTRACTBovine serum albumin (BSA) acts as a carrier for many endogenous and exogenous compounds, such as thyroid hormones or corresponding drugs. Binding of the hydrophilic compound levothyroxine (LT4) to BSA can significantly alter the pharmacological properties of the compound. Therefore, studying its interaction with BSA could be a difficult issue. In this work, the binding mechanism and affinity of the interaction between LT4 and BSA were investigated, both in solution using UV-Vis, Fourier-transform infrared spectroscopy (FT-IR), fluorescence and fluorescence resonance energy transfer (FRET), as well as by Surface Plasmon Resonance (SPR) with BSA confined to a gold-coated chips, as far as we know for the first time used to study the interactions between LT4 and proteins. Quenching of BSA fluorescence by LT4 combined with UV-Vis spectroscopy shows a ground-state complex formation that may be accompanied by a nonradiative energy transfer process. FT-IR revealed the changes induced by LT4 in the secondary structure of BSA molecules, due to the partial unfolding of BSA native structure upon LT4 binding. Scatchard approach allowed the determination of the binding constant and the thermodynamic parameters, which correspond to an enthalpic process, driven mainly by hydrogen bonds and van der Waals forces. Using SPR, the adsorbed amount of biomolecules was calculated and the binding affinity of LT4 with confined-BSA was characterized using the Hill-Langmuir equation, indicating that the BSA immobilization plays an important role in LT4 binding. As preliminary results, both fluorescence quenching and SPR can be used as a stepping stone for the development of a spectroscopic biosensor for LT4 detection, with a limit of detection as low as 0.23 × 10−6 M.

scholarly journals Spectroscopic and molecular docking elucidation to binding characteristics of bovine serum albumin with bupropion an aminoketone-medication for nicotine addiction

2019 ◽  
Vol 10 (2) ◽  
pp. 146-155
Author(s):  
Manjushree Makegowda ◽  
Revanasiddappa Hosakere Doddarevanna
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Circulatory System ◽  
Biologically Active ◽  
Binding Characteristics ◽  
Active Metal ◽  
Ft Ir ◽  
Binding Forces

One of the highly soluble protein presents in circulatory system of bovine body is bovine serum albumin (BSA). Bupropion hydrochloride (BRN) served to treat prime smoking cessation and disorder due to depressive. BRN binding to BSA was studied by molecular docking and lots of spectroscopic (UV-vis, emission, synchronous, 3D fluorescence, CD and FT-IR) methods at pH = 7.40. Static quenching with strong binding was obtained for BSA-BRN system by forming complex. Secondary structures, conformations and microenvironments of BSA were altered after BRN interaction. Distance between BRN and BSA was also achieved. Biologically active metal ions (Cu2+, Ca2+, Mg2+, Fe2+ and Zn2+) were also influenced on the BSA-BRN complex. Bonds of hydrogen and Van der Waals were major binding forces to stabilize BSA-BRN complex at site I (IIA) of BSA. Hence, binding of BRN to transport protein (BSA) is of prominent importance and these findings could be helpful for BRN pharmacology and potential clinical research.

scholarly journals Superior Performance of Magnetic Nanoparticles for Entrapment and Fixation of Bovine Serum Albumin In-Vitro

2020 ◽  
Vol 30 (4) ◽  
Author(s):  
Mansour Binandeh ◽  
Farrokh Karimi ◽  
Sadegh Rostamnia
Keyword(s):  
Magnetic Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Superior Performance ◽  
Precipitation Method ◽  
Experimental Conditions ◽  
Ft Ir ◽  
Co Precipitation

BACKGROUND: In recent years, extensive studies have been performed on magnetite nanoparticles (MNPs) and their applications, which have shown the current project to be one of the major applications by laboratory results.METHODS: The nanoparticles synthesized in this project were deposited by the co-precipitation method, which structure was identified by analyzers such as SEM, FT-IR, and EDX. The aim of this project is the adsorption and fixation of biomolecule (BSA (bovine serum albumin) protein on the surface of magnetic nanoparticles.RESULTS: The adsorption results by electrophoresis and spectrophotometric analyzers showed an absorption rate above 55% ie; 55% of the protein is fixed on the MNPs nanoparticles. This absorption is due to the high level of functionality of magnetic nanoparticles for adsorption of protein. The results of the EDX analysis also show the possible electrostatic bonding between the nanoparticles and the protein, this is derived from –OH with –NH2 groups of the nanobiocompound (MNPs /protein). After bonding, the two are easily separated.CONCLUSION: In this project, the Fe3O4 nanoparticles was synthesized and identified by SEM, FT-IR, and EDX analyzers and finally reacted with the BSA protein (for the absorption of protein on MNPs) under experimental conditions at a standard temperature of 25° C. The results showed that about 55% of the protein was fixed on magnetic nanoparticles.

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