The Effects of Drug Complexation on the Stability and Conformation of Human Serum Albumin: Protein Unfolding

2006 ◽  
Vol 45 (2) ◽  
pp. 203-214 ◽  
Author(s):  
A. Ahmed-Ouameur ◽  
S. Diamantoglou ◽  
M. R. Sedaghat-Herati ◽  
Sh. Nafisi ◽  
R. Carpentier ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Unfolding ◽  
The Stability

scholarly journals The Influence of Oxidative Stress on Serum Albumin Structure as a Carrier of Selected Diazaphenothiazine with Potential Anticancer Activity

2021 ◽  
Vol 14 (3) ◽  
pp. 285
Author(s):  
Małgorzata Maciążek-Jurczyk ◽  
Beata Morak-Młodawska ◽  
Małgorzata Jeleń ◽  
Wiktoria Kopeć ◽  
Agnieszka Szkudlarek ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Anticancer Activity ◽  
Drug Distribution ◽  
Cd Spectroscopy ◽  
Drug Binding ◽  
Protein Activity ◽  
Chloramine T ◽  
The Stability

Albumin is one of the most important proteins in human blood. Among its multiple functions, drug binding is crucial in terms of drug distribution in human body. This protein undergoes many modifications that are certain to influence protein activity and affect its structure. One such reaction is albumin oxidation. Chloramine T is a strong oxidant. Solutions of human serum albumin, both non-modified and modified by chloramine T, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. 10H-3,6-diazaphenothiazine (DAPT) has anticancer activity and it has been studied for the first time in terms of binding with human serum albumin—its potential as a transporting protein. Using fluorescence spectroscopy, in the presence of dansylated amino acids, dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), DAPT binding with two main albumin sites—in subdomain IIA and IIIA—has been evaluated. Based on the conducted data, in order to measure the stability of DAPT complexes with human (HSA) and oxidized (oHSA) serum albumin, association constant (Ka) for ligand-HSA and ligand-oHSA complexes were calculated. It has been presumed that oxidation is not an important issue in terms of 10H-3,6-diazaphenothiazine binding to albumin. It means that the distribution of this substance is similar regardless of changes in albumin structure caused by oxidation, natural occurring in the organism.

Comparison of the stability of Y-90-, Lu-177- and Ga-68- labeled human serum albumin microspheres (DOTA-HSAM)

2010 ◽  
Vol 37 (8) ◽  
pp. 861-867 ◽  
Author(s):  
Gerd Wunderlich ◽  
Eik Schiller ◽  
Ralf Bergmann ◽  
Hans-Jürgen Pietzsch
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Microspheres ◽  
The Stability

Fluorescence studies by quenching and protein unfolding on the interaction of bioactive compounds in water extracts of kiwi fruit cultivars with human serum albumin

2015 ◽  
Vol 160 ◽  
pp. 71-77 ◽  
Author(s):  
Yong Seo Park ◽  
Martin Polovka ◽  
Alma Leticia Martinez-Ayala ◽  
Gustavo A. González-Aguilar ◽  
Kyung-Sik Ham ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bioactive Compounds ◽  
Protein Unfolding ◽  
Kiwi Fruit ◽  
Fluorescence Studies ◽  
Water Extracts

scholarly journals Human Serum Albumin Increases the Stability of Green Tea Catechins in Aqueous Physiological Conditions

PLoS ONE ◽  
2015 ◽  
Vol 10 (7) ◽  
pp. e0134690 ◽  
Author(s):  
Angelo Zinellu ◽  
Salvatore Sotgia ◽  
Bastianina Scanu ◽  
Mauro Forteschi ◽  
Roberta Giordo ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Green Tea ◽  
Tea Catechins ◽  
Physiological Conditions ◽  
Green Tea Catechins ◽  
The Stability

scholarly journals Chemical and Physical Characterisation of Human Serum Albumin Nanocolloids: Kinetics, Strength and Specificity of Bonds with 99mTc and 68Ga

Nanomaterials ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1776
Author(s):  
Manuela Marenco ◽  
Letizia Canziani ◽  
Gianluca De Matteis ◽  
Giorgio Cavenaghi ◽  
Carlo Aprile ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Degradation Products ◽  
Wide Spectrum ◽  
Ph Effect ◽  
Physicochemical Characteristics ◽  
Multiple Binding Sites ◽  
Commercial Kits ◽  
The Stability

Nanoparticles of Human Serum Albumin (NC) labelled with 99mTc are widely used in Nuclear Medicine and represent the gold-standard for the intraoperative detection of the sentinel lymph node in many kinds of cancer, mainly breast cancer and melanoma. A significant amount of radionuclides can be incorporated into the HSA particle, due to the multiple binding sites, and HSA-based nanocolloid catabolism is a fast and easy process that results in innocuous degradation products. NCs labelled with different isotopes represent an interesting radiopharmaceutical for extending diagnostic accuracy and surgical outcome, but the knowledge of the chemical bond between NCs and isotopes has not been fully elucidated, including information on its strength and specificity. The aim of this study is to investigate and compare the physicochemical characteristics of the bond between NCs and 99mTc and 68Ga isotopes. Commercial kits of HSA-based nanocolloid particles (NanoAlbumon®) were used. For this purpose, we have primarily studied the kinetic orders of NC radiolabelling. Langmuir isotherms and pH effect on radiolabelling were tested and the stability of the radiometal complex was verified through competition reactions carried out in presence of different ligands. The future goal of our research is the development of inexpensive and instant kits, easily labelled with a wide spectrum of diagnostic and therapeutic isotopes, thus facilitating the availability of versatile and multipurpose radiopharmaceuticals.

scholarly journals Protein-templated copper nanoclusters for fluorimetric determination of human serum albumin

2021 ◽  
Vol 188 (4) ◽  
Author(s):  
Mariagrazia Lettieri ◽  
Pasquale Palladino ◽  
Simona Scarano ◽  
Maria Minunni
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescent Detection ◽  
Fluorimetric Determination ◽  
Copper Nanoclusters ◽  
Optical Reporters ◽  
The Stability ◽  
Serum And Urine

AbstractCopper nanoclusters (CuNCs) are attractive for their unique optical properties, providing sensitive fluorescent detection of several kinds of targets even in complex matrices. Their ability in growing on suitable protein and nucleic acid templates make CuNCs efficient optical reporters to be exploited in bioanalysis. In this work, we report the specific and sensitive determination of human serum albumin (HSA) in human serum (HS) and urine via CuNCs fluorescence. HSA is the most abundant protein in plasma, and plays a key role in the early diagnosis of serious pathological conditions such as albuminuria and albuminemia. Recently, HSA has become clinically central also as a biomarker to assess severity, progression, and prognosis of various cancers. We report the controlled and reproducible growth of CuNCs directly on the target analyte, HSA, which results in a fine dose-dependent fluorescent emission at 405 nm. The protocol is optimized in water, and then applied to serum and urine specimens, without matrix pretreatment. The method linearly responds within the whole concentration of clinical interest, with a sensitivity of 1.8 ± 0.1 × 10−3 g L−1 and 0.62 ± 0.03 × 10−3 g L−1 in serum and urine, respectively, and excellent reproducibility (CVav% ca. 3% for both). The assay is designed to have a single protocol working for both matrices, with recovery of 95% (HS) and 96% (urine). The stability of the fluorescence after CuNCs formation was tested over 3 days, displaying good results (yet higher in urine than in serum). Graphical abstract

scholarly journals Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with 99mTc and 68Ga

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 404
Author(s):  
Letizia Canziani ◽  
Manuela Marenco ◽  
Giorgio Cavenaghi ◽  
Giulia Manfrinato ◽  
Angelo Taglietti ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Efficiency ◽  
Physical Chemical ◽  
Size Dimension ◽  
Commercial Kits ◽  
The Stability ◽  
Optimal Ph

Background: Macroaggregated human serum albumin (MAA) properties are widely used in nuclear medicine, labelled with 99mTc. The aim of this study is to improve the knowledge about the morphology, size, dimension and physical–chemical characteristics of MAA and their bond with 99mTc and 68Ga. Methods: Commercial kits of MAA (Pulmocis®) were used. Characterisation through experiments based on SEM, DLS and Stokes’ Law were carried out. In vitro experiments for Langmuir isotherms and pH studies on radiolabelling were performed and the stability of the radiometal complex was verified through competition reactions. Results: The study settles the MAA dimension within the range 43–51 μm. The Langmuir isotherm reveals for [99mTc]MAA: Bmax (46.32), h (2.36); for [68Ga]MAA: Bmax (44.54), h (0.893). Dual labelling reveals that MAA does not discriminate different radioisotopes. Experiments on pH placed the optimal pH for labelling with 99mTc at 6. Conclusion: Radiolabelling of MAA is possible with high efficiency. The nondiscriminatory MAA bonds make this drug suitable for radiolabelling with different radioisotopes or for dual labelling. This finding illustrates the need to continue investigating MAA chemical and physical characteristics to allow for secure labelling with different isotopes.

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