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.

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.

A new drug binding subsite on human serum albumin and drug–drug interaction studied by X-ray crystallography

2008 ◽  
Vol 162 (1) ◽  
pp. 40-49 ◽  
Author(s):  
Lili Zhu ◽  
Feng Yang ◽  
Liqing Chen ◽  
Edward J. Meehan ◽  
Mingdong Huang
Keyword(s):  
Drug Interaction ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Drug Binding ◽  
X Ray ◽  
X Ray Crystallography ◽  
New Drug ◽  
Drug Drug Interaction

Bis(1-phenyl-1-propyne) complexes of tungsten(II): crystal structures of [WI2(CO)(NCR)(η2-MeC2Ph)2] (R = Me, Et, or Ph)

2001 ◽  
Vol 79 (3) ◽  
pp. 263-271
Author(s):  
Paul K Baker ◽  
Michael GB Drew ◽  
Deborah S Evans
Keyword(s):  
Carbon Monoxide ◽  
Solid State ◽  
Crystal Structures ◽  
Octahedral Geometry ◽  
X Ray ◽  
X Ray Crystallography ◽  
Alkyne Complexes ◽  
First Time

Reaction of [WI2(CO)3(NCMe)2] with two equivalents of 1-phenyl-1-propyne (MeC2Ph) in CH2Cl2, and in the absence of light, gave the bis(1-phenyl-1-propyne) complex [WI2(CO)(NCMe)(η2-MeC2Ph)2] (1) in 77% yield. Treatment of equimolar quantities of 1 and NCR (R = Et, i-Pr, t-Bu, Ph) in CH2Cl2 afforded the nitrile-exchanged products, [WI2(CO)(NCR)(η2-MeC2Ph)2] (2-5) (R = Et (2), i-Pr (3), t-Bu (4), Ph (5)). Complexes 1, 2, and 5 were structurally characterized by X-ray crystallography. All three structures have the same pseudo-octahedral geometry, with the equatorial sites being occupied by cis and parallel alkyne groups, which are trans to the cis-iodo groups. The trans carbon monoxide and acetonitrile ligands occupy the axial sites. In structures 1 and 2, the methyl and phenyl substituents of the 1-phenyl-1-propyne ligands are cis to each other, whereas for the bulkier NCPh complex (5), the methyl and phenyl groups are trans to one another. This is the first time that this arrangement has been observed in the solid state in bis(alkyne) complexes of this type.Key words: bis(1-phenyl-1-propyne), carbonyl, nitrile, diiodo, tungsten(II), crystal structures.

Spectroscopic and molecular modeling studies of human serum albumin interaction with propyl gallate

RSC Advances ◽  
2014 ◽  
Vol 4 (110) ◽  
pp. 64559-64564 ◽  
Author(s):  
Jafar Ezzati Nazhad Dolatabadi ◽  
Vahid Panahi-Azar ◽  
Abolfazl Barzegar ◽  
Ali Akbar Jamali ◽  
Fahimeh Kheirdoosh ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Propyl Gallate ◽  
Fluorescence Quenching Method ◽  
Molecular Modeling Studies ◽  
Quenching Method ◽  
First Time

For the first time, PG interaction with HSA using fluorescence quenching method, circular dichroism spectroscopy and molecular modeling was investigated.

scholarly journals Sesquiterpene Lactones from Inula oculus-christi

2010 ◽  
Vol 5 (4) ◽  
pp. 1934578X1000500 ◽  
Author(s):  
Mahmoud Mosaddegh ◽  
Maryam Hamzeloo Moghadam ◽  
Saeedeh Ghafari ◽  
Farzaneh Naghibi ◽  
Seyed Nasser Ostad ◽  
...  
Keyword(s):  
Cytotoxic Activity ◽  
Crystal Structures ◽  
Spectroscopic Data ◽  
Sesquiterpene Lactones ◽  
X Ray ◽  
X Ray Crystallography ◽  
First Time

Inula oculus-christi L. (Compositae) extract was chromatographed and three sesquiterpene lactones ergolide, gaillardin and pulchellin C were isolated. The structures of these compounds were determined by analysis of their spectroscopic data, and their crystal structures were defined using X-ray crystallography; the isolation of ergolide and pulchellin C is reported for the first time from this species. These three compounds were evaluated for their in vitro cytotoxic activity against MDBK, MCF7 and WEHI164 cells; ergolide and gaillardin exhibited lower and significantly different IC50 values compared with pulchellin C ( p<0.001).

Structural study of the glycosylated and unglycosylated forms of a genetic variant of human serum albumin (63 Asp → Asn)

1995 ◽  
Vol 1252 (2) ◽  
pp. 209-216 ◽  
Author(s):  
Yasushi Sakamoto ◽  
Kunio Kitamura ◽  
Jeanne Madison ◽  
Scott Watkins ◽  
Carl-Bertil Laurell ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structural Study ◽  
Genetic Variant

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
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