Adsorption behavior of human serum albumin on ATR crystal studied by in situ ATR/FTIR spectroscopy and two-dimensional correlation analysis

The Analyst ◽  
2011 ◽  
Vol 136 (8) ◽  
pp. 1747 ◽  
Author(s):  
He Huang ◽  
Jing Xie ◽  
Hong Chen
Keyword(s):  
Human Serum Albumin ◽  
Correlation Analysis ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Adsorption Behavior ◽  
Two Dimensional

scholarly journals Development of In Situ Gelling Meloxicam-Human Serum Albumin Nanoparticle Formulation for Nose-to-Brain Application

Pharmaceutics ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 646
Author(s):  
Gábor Katona ◽  
Bence Sipos ◽  
Mária Budai-Szűcs ◽  
György Tibor Balogh ◽  
Szilvia Veszelka ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nasal Mucosa ◽  
Drug Absorption ◽  
Cell Damage ◽  
Lipid Fraction ◽  
Poloxamer 407 ◽  
Nasal Drug Delivery

The aim of this study was to develop an intranasal in situ thermo-gelling meloxicam-human serum albumin (MEL-HSA) nanoparticulate formulation applying poloxamer 407 (P407), which can be administered in liquid state into the nostril, and to increase the resistance of the formulation against mucociliary clearance by sol-gel transition on the nasal mucosa, as well as to improve drug absorption. Nanoparticle characterization showed that formulations containing 12–15% w/w P407 met the requirements of intranasal administration. The Z-average (in the range of 180–304 nm), the narrow polydispersity index (PdI, from 0.193 to 0.328), the zeta potential (between −9.4 and −7.0 mV) and the hypotonic osmolality (200–278 mOsmol/L) of MEL-HSA nanoparticles predict enhanced drug absorption through the nasal mucosa. Based on the rheological, muco-adhesion, drug release and permeability studies, the 14% w/w P407 containing formulation (MEL-HSA-P14%) was considered as the optimized formulation, which allows enhanced permeability of MEL through blood–brain barrier-specific lipid fraction. Cell line studies showed no cell damage after 1-h treatment with MEL-HSA-P14% on RPMI 2650 human endothelial cells’ moreover, enhanced permeation (four-fold) of MEL from MEL-HSA-P14% was observed in comparison to pure MEL. Overall, MEL-HSA-P14% can be promising for overcoming the challenges of nasal drug delivery.

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

Two-dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

1995 ◽  
Vol 16 (1) ◽  
pp. 851-853 ◽  
Author(s):  
Barbara Marzocchi ◽  
Barbara Magi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Inhibition of Human Serum Albumin Fibrillation by Two-Dimensional Nanoparticles

2017 ◽  
Vol 121 (22) ◽  
pp. 5474-5482 ◽  
Author(s):  
Sudipta Bag ◽  
Rishav Mitra ◽  
Sunando DasGupta ◽  
Swagata Dasgupta
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Two Dimensional

Microdynamic changes of moisture-induced crystallization of amorphous calcium carbonate revealed via in situ FTIR spectroscopy

2019 ◽  
Vol 21 (39) ◽  
pp. 21882-21889 ◽  
Author(s):  
Meng Cheng ◽  
Shengtong Sun ◽  
Peiyi Wu
Keyword(s):  
Calcium Carbonate ◽  
Correlation Analysis ◽  
Ftir Spectroscopy ◽  
Two Dimensional ◽  
In Situ Ftir ◽  
Amorphous Calcium Carbonate ◽  
In Situ Ftir Spectroscopy ◽  
Induced Crystallization

A microdynamic mechanism of moisture-induced ACC crystallization involving three consecutive conversion stages is elucidated via in situ FTIR spectroscopy and two-dimensional correlation analysis.

Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy

Chirality ◽  
2014 ◽  
Vol 26 (9) ◽  
pp. 497-501 ◽  
Author(s):  
Andrea N. L. Batista ◽  
João M. Batista ◽  
Lorna Ashton ◽  
Vanderlan S. Bolzani ◽  
Maysa Furlan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Optical Activity ◽  
Conformational Transitions ◽  
Two Dimensional ◽  
Raman Optical Activity
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