X-ray photoelectron spectroscopy as a tool for studies of the surface layer of microspheres. The case of polystyrene and poly(styrene-acrolein) microspheres with attached human serum albumin

2000 ◽  
Vol 278 (9) ◽  
pp. 878-883 ◽  
Author(s):  
S. Slomkowski ◽  
D. Kowalczyk ◽  
M. M. Chehimi ◽  
M. Dealamar
Keyword(s):  
Surface Layer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Photoelectron Spectroscopy ◽  
X Ray

scholarly journals Investigation of the surface layer of 3D-matrices for tissue engineering

2017 ◽  
Vol 63 (1) ◽  
pp. 32-38 ◽  
Author(s):  
V.S. Chernonosova ◽  
R.I. Kvon ◽  
E.V. Kiseleva ◽  
A.O. Stepanova ◽  
P.P. Laktionov
Keyword(s):  
Tissue Engineering ◽  
Surface Layer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Photoelectron Spectroscopy ◽  
Proteinase K ◽  
Protein Distribution ◽  
Natural Polymers ◽  
X Ray

Electrospinning is a convenient and promising manufacturing method a variety of materials for tissue engineering. 3D matrices fabricated by electrospinning from solutions of polycaprolactone with human serum albumin or gelatin in 1,1,1,3,3,3-hexafluoroisopropanol were studied. The microstructure of the 3D matrices and surface of the fibers were investigated using scanning electron microscopy. Protein distribution in the surface layer was studied by modification of protein amino groups with N-(2-hydroxyethyl)phenazine and X-ray photoelectron spectroscopy. It was shown, that concentration of the proteins in the surface layer of fibers exceeded their concentration in the initial electrospun solution up to 12 times and the surface layer was enriched in the protein inversely to the concentration of the protein in solution. The minor part of the proteins was released from fibers during first 30-60 min after swelling in water. Treatment of matrices with proteinase K hydrolyzed about 1/3 of the surface exposed human serum albumin. Thus, both methods can be used to study the surface content of the materials produced by electrospinning from blends of synthetic and natural polymers, however X-ray photoelectron spectroscopy appears to be more convenient and informative.

scholarly journals In Silico Prediction of Interactions between Site II on Human Serum Albumin and Profen Drugs

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Hideto Isogai ◽  
Noriaki Hirayama
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Mode ◽  
X Ray ◽  
Docking Simulations ◽  
X Ray Crystallography ◽  
Inflammatory Drugs ◽  
Multiple Template

Since binding of a drug molecule to human serum albumin (HSA) significantly affects the pharmacokinetics of the drug, it is highly desirable to predict the binding affinity of the drug. Profen drugs are a widely used class of nonsteroidal anti-inflammatory drugs and it has been reported that several members of the profen class specifically bind to one of the main binding sites named site II. The actual binding mode of only ibuprofen has been directly confirmed by X-ray crystallography. Therefore, it is of interest whether other profen drugs are site II binders. Docking simulations using multiple template structures of HSA from three crystal structures of complexes between drugs and HSA have demonstrated that most of the currently available profen drugs should be site II binders.

scholarly journals Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry

2005 ◽  
Vol 387 (3) ◽  
pp. 695-702 ◽  
Author(s):  
Bill X. HUANG ◽  
Chhabil DASS ◽  
Hee-Yong KIM
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Cross Linking ◽  
X Ray ◽  
Chemical Cross Linking

Mass spectrometry with chemical cross-linking was used to probe the conformational changes of HSA (human serum albumin) in solution on interaction with monounsaturated OA (oleic acid) or polyunsaturated AA (arachidonic acid) or DHA (docosahexaenoic acid). Fatty acid-free or -bound HSA was modified with lysine-specific cross-linkers and digested with trypsin. Cross-linked peptides were analysed by nano-electrospray ionization MS to localize the sites of cross-linking. Our data indicated that a local conformational change involving movement of the side chains of Lys-402 of subdomain IIIA or Lys-541 of subdomain IIIB occurred upon binding of all three fatty acids. Our data also indicated that the side chains of Lys-205 (IIA) and Lys-466 (IIIA) moved closer towards each other upon binding AA or DHA, but not OA, suggesting that the conformations of HSA when bound to mono- and poly-unsaturated fatty acids are distinctively different. While these observations agreed with previous X-ray crystallographic studies, the distances between ε-amino groups of most cross-linked lysine pairs were shorter than the crystal structure predicted, possibly reflecting a discrepancy between the solution and crystal structures. This method can serve as a useful complement to X-ray crystallography, particularly in probing the structure of a protein in solution.

Human Serum Albumin Unfolding: A Small-Angle X-ray Scattering and Light Scattering Study

2008 ◽  
Vol 112 (48) ◽  
pp. 15460-15469 ◽  
Author(s):  
Luciano Galantini ◽  
Claudia Leggio ◽  
Nicolae Viorel Pavel
Keyword(s):  
Light Scattering ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study ◽  
Ray Scattering

Neutron and X-ray Reflectivity Studies of Human Serum Albumin Adsorption onto Functionalized Surfaces of Self-Assembled Monolayers

1997 ◽  
Vol 13 (5) ◽  
pp. 635-639 ◽  
Author(s):  
S. Petrash ◽  
A. Liebmann-Vinson ◽  
M.D. Foster ◽  
L.M. Lander ◽  
W.J. Brittain ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Self Assembled Monolayers ◽  
X Ray ◽  
Functionalized Surfaces ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Albumin Adsorption

Cisplatin binding to human serum albumin: a structural study

2015 ◽  
Vol 51 (46) ◽  
pp. 9436-9439 ◽  
Author(s):  
Giarita Ferraro ◽  
Lara Massai ◽  
Luigi Messori ◽  
Antonello Merlino
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Crystal Structures ◽  
Structural Study ◽  
X Ray ◽  
X Ray Crystallography ◽  
First Time

The reaction between cisplatin and human serum albumin (HSA) was investigated by X-ray crystallography and crystal structures of the cisplatin/HSA adduct were eventually solved for the first time.

Solution equilibria and the X-ray structure of Cu(ii) complexation with 3-amino-N-(pyridin-2-ylmethyl)propanamide, a pseudo-mimic of human serum albumin

2016 ◽  
Vol 45 (42) ◽  
pp. 17010-17019 ◽  
Author(s):  
Graham E. Jackson ◽  
Fatin M. Elmagbari ◽  
Ahmed N. Hammouda ◽  
Raffaele P. Bonomo
Keyword(s):  
Rheumatoid Arthritis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Copper Complexes ◽  
Inflammatory Activity ◽  
X Ray ◽  
Solution Equilibria ◽  
Anti Inflammatory

Copper complexes have anti-inflammatory activity in the treatment of inflammation associated with rheumatoid arthritis (RA).

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