scholarly journals Redox Homeostasis of Albumin in Relation to Alpha-Lipoic Acid and Dihydrolipoic Acid

2010 ◽  
Vol 3 (3) ◽  
pp. 206-213 ◽  
Author(s):  
Pinar Atukeren ◽  
Seval Aydin ◽  
Ezel Uslu ◽  
MKoray Gumustas ◽  
Ufuk Cakatay
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lipoic Acid ◽  
Protein Oxidation ◽  
Antioxidant Properties ◽  
Oxidative Modification ◽  
Breakdown Product ◽  
Alpha Lipoic Acid ◽  
Dihydrolipoic Acid

Albumin represents the predominant circulating antioxidant agent in plasma exposed to continuous oxidative stress and a change in serum albumin structure accounts for its antioxidant properties. Alterations in the redox status of albumin may result in impairments of its biological properties. Alpha-lipoic acid (LA), a naturally occurring thiol compound found in virtually all species, is a potent antioxidant with high efficacy which is also involved in the chelation of metal ions, regeneration of antioxidants, and repair of oxidatively damaged proteins. In human body LA is rapidly reduced to dihydrolipoic acid (DHLA) after intake into the cell. Both, LA and DHLA are amphipathic molecules which act as antioxidants both in hydrophilic and lipophilic environments. The present study aimed to investigate the antioxidant/pro-oxidant effects of LA and DHLA due to their concentrations in metal-catalyzed protein oxidation (MCO) of human serum albumin (HSA). Progressive oxidative modification of albumin was found in MCO system by an increased content of protein hydroperoxides (POOH), protein carbonyl groups (PCO) which is the former's major breakdown product, and other protein oxidation markers such as advanced oxidized protein products (AOPP) and protein thiol groups (P-SH). The possible antioxidant protective effects of LA and DHLA were observed with 25 µM and 50 µM; DHLA being more influential. Protein oxidation parameters were found to be lower and P-SH levels seemed higher. However, prooxidant effects of both LA and DHLA came on the scene with increased concentrations of 75 µM and 100 µM where the latter seemed the most hazardous with contradicted results. It is clear that the loss of biological activity of human serum albumin by MCO system appears of medical relevance and if LA exerts similar effects seen in the present study, it is possible that cellular prooxidant activity can also result consuming this unique antioxidant in certain doses.

scholarly journals Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approach

2021 ◽  
pp. 41-41
Author(s):  
Nikola Gligorijevic ◽  
Vladimir Sukalovic ◽  
Simeon Minic ◽  
Goran Miljus ◽  
Olgica Nedic ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lipoic Acid ◽  
Food Supplement ◽  
Alpha Lipoic Acid ◽  
Salt Bridges ◽  
Preferential Binding ◽  
Docking Approach

The binding of popular food supplement and a well-known anti-oxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00?0.05?104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that Sudlow I site could accommodate DHLA and ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, the knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation.

scholarly journals Dihydro-alpha-lipoic acid binds to human serum albumin at Sudlow I binding site

2020 ◽  
Author(s):  
Nikola Gligorijević ◽  
Vladimir Šukalović ◽  
Goran Miljuš ◽  
Olgica Nedić ◽  
Ana Penezić
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Lipoic Acid ◽  
Electrostatic Interactions ◽  
Dietary Intervention ◽  
Alpha Lipoic Acid ◽  
Preferential Binding

ABSTRACTBinding of dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised in detail in this study. Binding process was monitored by spectroscopic methods and molecular docking approach. HSA binds DHLA with moderate affinity, 0.80 ± 0.007 × 104 M−1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Hydrogen bonds and electrostatic interactions were identified as the key binding interactions. DHLA binding thermally stabilized HSA, yet it had no effect on HSA structure and its susceptibility to trypsin digestion. Molecular docking confirmed that Sudlow I site accommodated DHLA in a certain conformation in order for binding to occur. Molecular dynamic simulation showed that formed complex is stable. Reported results offer future perspectives for investigations regarding the use of DHLA as a dietary intervention but also raise concerns about the effectiveness of alpha-lipoic acid and DHLA in treatment of patients with COVID-19.

scholarly journals The effect of cupric and ferric ions on antioxidant properties of human serum albumin

2014 ◽  
Vol 33 (04) ◽  
pp. 453-456
Author(s):  
Gholamreza Rezaei Behbehani ◽  
Katayon Gonbadi ◽  
Nasrin Eslami
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Antioxidant Properties ◽  
Ferric Ions

scholarly journals Specific antioxidant properties of human serum albumin

2013 ◽  
Vol 3 (1) ◽  
pp. 4 ◽  
Author(s):  
Myriam Taverna ◽  
Anne-Lise Marie ◽  
Jean-Paul Mira ◽  
Bertrand Guidet
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Antioxidant Properties

scholarly journals Lipoic acid capped silver nanoparticles: a facile route to covalent protein capping and oxidative stability within biological systems

RSC Advances ◽  
2020 ◽  
Vol 10 (54) ◽  
pp. 32953-32958
Author(s):  
Irene Guzmán-Soto ◽  
Mary Omole ◽  
Emilio I. Alarcon ◽  
Christopher D. McTiernan
Keyword(s):  
Silver Nanoparticles ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Oxidative Stability ◽  
Human Serum ◽  
Lipoic Acid ◽  
Surface Composition ◽  
Biological Systems ◽  
Covalent Attachment ◽  
Facile Route

Covalent attachment of human serum albumin protein to the surface of spherical lipoic acid capped silver nanoparticles results in the generation of stable nanoparticle–protein hybrids with well defined surface composition.

Binding of α-lipoic acid to human serum albumin: spectroscopic and molecular modeling studies

2021 ◽  
Author(s):  
Fatemeh Toosi-Moghadam ◽  
Mehdi Khoobi ◽  
Ali Akbar Saboury ◽  
Zahra Allahdad ◽  
Anahita Khammari ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lipoic Acid ◽  
Modeling Studies ◽  
Molecular Modeling Studies

II. Lokalisation der Placenta mit 113Inm- Human-Serum-Albumin

1969 ◽  
Vol 08 (01) ◽  
pp. 15-21 ◽  
Author(s):  
K. E. Scheer ◽  
J. Heep ◽  
W. Maier-Borst ◽  
W. J. Lorenz ◽  
H. Sinn ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Vena Cava ◽  
Placenta Praevia ◽  
Wird Eine

ZusammenfassungNach tierexperimentellen Voruntersuchungen wurde die Placentographie mit trägerfreiem 113Inm -HSA als klinische Methode eingeführt. Vor Amniocentesen und bei Verdacht auf Placenta praevia werden Placentographien geschrieben. Den Schwangeren wird eine Aktivität von 500 μCi in die Cubitalvene injiziert. Die der Aktivität entsprechende Indiummenge ist kleiner als 0,1 ng. Die fetale Strahlenbelastung liegt unter lOmrad. Bei Anwendung von 113Inm-HSA entfällt eine Blockade der mütterlichen und fetalen Schilddrüsen. Die genaue Abgrenzung einer Placenta praevia wird nicht durch eine Blasenaktivität beeinträchtigt.Es wurden bisher 19 Placentalokalisationen durchgeführt. In allen Fällen konnte der Placentasitz eindeutig festgestellt werden. Bedingt durch die lange Liegezeit beim Aufnehmen eines Szintigramms kam es in zwei Fällen zu einem Vena-Cava-Kompressions-Syndrom. Zur Verhinderung dieser klinischen Zwischenfälle werden inzwischen Placentographien mit der Anger-Kamera aufgenommen. Mit Hilfe des divergierenden Kollimators konnte der gesamte Abdominalbereich erfaßt werden. Die Aufnahmezeit konnte auf 7 — 10 Minuten verkürzt werden. Die intravenöse injizierte Aktivität betrug bei dieser Methode ebenfalls 500 μCi. Der diagnostische Aussagewert der Kamerabilder ist szintigraphischen Aufnahmen gleichwertig.

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