Human Serum Albumin Hsa
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Human Serum Albumin Hsa
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Author : Travis Stokes
language : en
Publisher: Nova Science Publishers
Release Date : 2015
Human Serum Albumin Hsa written by Travis Stokes and has been published by Nova Science Publishers this book supported file pdf, txt, epub, kindle and other format this book has been release on 2015 with Serum albumin categories.
Human Serum Albumin (HSA) is the most abundant plasma protein. It has been widely used for drug delivery systems and has recently emerged as a versatile carrier for therapeutic agents against diabetes, cancer and infectious diseases. This book provides an overview of the expanding field of preclinical and clinical applications and developments that use albumin as a carrier of drug delivery systems. The authors' discuss the properties of drug binding sites within the structure of HSA, discuss new possibilities for the therapeutic potential of HSA and analyze recently reported HSA-drug complexes including HSA-antibody conjugates. Novel investigations on the applications of albumin fusion proteins are discussed as well, with a focus on tumor targeting and intracellular delivery. Other chapters examine the different aspects of albumin glycation and oxidation, the changes in the structure of human serum albumin determined from infrared spectroscopy and a review of CAPIDAN, a special fluorescent dye, which attaches to drug binding sites of human serum albumin.
Albumin In Medicine
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Author : Masaki Otagiri
language : en
Publisher: Springer
Release Date : 2016-11-01
Albumin In Medicine written by Masaki Otagiri and has been published by Springer this book supported file pdf, txt, epub, kindle and other format this book has been release on 2016-11-01 with Medical categories.
This book presents a comprehensive overview of medical and pharmaceutical applications of human serum albumin (HSA), with updates on structural aspects of albumin from the perspectives of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in various pathological conditions, and genetic variants and their phenotypes. Rapid progress and development of its applications have resulted in outstanding results for which albumin has clearly been proven to be a robust biomaterial. Contributions from leading international experts in this field show how HSA is applied to diagnosis, therapy, drugs, and treatment, with a comprehensive introduction of HSA. This volume will appeal to scientists in pharmaceutical and medical research including pharmaceutical chemists, pharmacokineticists, toxicologists, and biochemists not only in academia but also in industry. Readers can effectively acquire the most recent knowledge of applications of HSA and its impact on human health in a single volume.
Transanalysis Of Human Serum Albumin Function Based On Evolutionarily And Experimentally Unique Amino Acids
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Author : Sean Artello
language : en
Publisher:
Release Date : 2018
Transanalysis Of Human Serum Albumin Function Based On Evolutionarily And Experimentally Unique Amino Acids written by Sean Artello and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2018 with categories.
Human serum albumin (HSA) is a predominant blood protein with binding affinity to many endogenous and exogenous compounds. Following an overview of this protein, the additional capacity for heme binding is analyzed as both an evolutionarily retained and experimentally inducible function. An inclusive analysis of HSA has examined all facets of HSAs current structure, potential variations of this structure that may be induced experimentally, and the potential for evolutionary selection regarding beneficial variance. Initial background information was analyzed including structure and function, the role of HSA within the body, and medical applications, including a proposal for protein modification to facilitate the new application of heme binding and oxygen carrying ability. Once these variations were reviewed, 10 different species (mammalian, reptilian, and avian) were examined for conserved or new heme binding functionality within five relevant heme binding regions. Analysis at these regions, positions 138, 142, 146, 161, and 190 showed relative conservation, but the potential for heme binding as an accommodation for oxidative stress appears negligible within these species. Following this evaluation, procedure and methodology was outlined for the generation of mutant HSA plasmid and possible routes of generating mutant HSA protein with heme binding capability.
Cys34 Thiol Group Of Human Serum Albumin Possibilities And Importance Of Determination In Clinical Practise
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Author :
language : en
Publisher:
Release Date : 2013
Cys34 Thiol Group Of Human Serum Albumin Possibilities And Importance Of Determination In Clinical Practise written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2013 with categories.
Human serum albumin (HSA) has a multitude of physiological functions, and one of them is to defend the organism against oxidative and/or carbonyl stress. This prominent function is enabled by the presence of single free Cys34 thiol group at the surface of HSA molecules. Determination of HSA-SH group content could be a suitable parameter for oxidative and/or carbonyl stress level assesemnet in different pathological states. In order to become aplicable in clinical practice, it is necessary to isolate HSA from serum or plasma in the first, and then to determine the content of thiol group. Monitoring of the reliability of affinity chromatography with Cibacron Blue (CB) for HSA isolation from serum of healthy and diabetic persons, and thiol group quantification, showed that HSA-SH group content was higher from 6 to 33% than the total serum thiols content, i.e. that the accuracy of this method is low (HSA-SH group content recovery ranging from 113.6 to 130.1%). This discrepancy is not caused by the isolation conditions (sample volume, matrix charateristics, column flow and the time needed for HSA isolation and SH group content determination), presence of buffer for HSA isolation and other proteins in isolated HSA preparation (purity range from 88.4 to 91.4%), influence of proteins, small molecules and ions present in the serum on the HSA-SH content determination, but the selection of HSA molecules by CB according to their conformations. The change in conformation (determined by emmission flourescent spectroscopy and CD), and accordingly the selection, depend on the type and the number of fatty acid (FA) molecules bound to HSA. Besides that, the nautre and the number of HSA bound FAs contribute to the increase in HSA-SH group reactivity: pseudo-first order rate constant for the reaction HSA-SH group with DTNB in CB bound fraction (21.74x10-3 s-1) is higher compared to unbound HSA fraction (11.2x10-3 s-1), as well as in diabetic group (n=20) (20.9x10-3 s-1) compared to the
Human Serum Albumin
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Author : Dianne Cohen
language : en
Publisher:
Release Date : 2019
Human Serum Albumin written by Dianne Cohen and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2019 with Albumins categories.
Human serum albumin is found in the intravascular and extracellular space and is the main protein of human blood plasma. Human serum albumin binds water, cations (such as Ca2+, Na+, K+), fatty acids, hormones, bilirubin, thyroxin (T4) and pharmaceuticals. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds. In the opening chapter of Human Serum Albumin: Structure, Binding and Activity the authors review, the structure, content and binding of HSA.Then, the role of albumin in free radical trapping activities and as an oxyradical scavenger is described. A discussion of recent advances in the use of the antioxidant properties of human serum albumin to make drugs detectable in vivo is also presented.Human serum albumin has one tryptophan residue and shows a characteristic fluorescence of around 350 nm under ultraviolet irradiation. Because tryptophan is easily oxidized by reactive oxygen species and/or photoexcited molecules through electron transfer (leading to fluorescence diminishment) a fluorometry of this tryptophan residue is a useful tool to evaluate oxidation. In light of these characteristics, the authors examine the photosensitizing activity of organic photosensitizers, including porphyrins and phenothiazine dyes.The use of magnetic resonance imaging and spectroscopy for the determination of human serum albumin structure, drug binding and in vivo activity is explored, in addition to drug modifications using human serum albumin.Following this, this compilation studies the major approaches for the characterization of human serum albumin as a fluorinated drug delivery agent and fluorinated albumin influence on drug binding. Synthesis and characterization of fluorinated conjugates of albumin and adsorbed human serum albumin on surfaces containing CF3 are also discussed.The concluding study investigates possible similarities and differences in albumin concentration and the presence of tyrosine in urine from a population of healthy and microalbuminuria dependent women. The assessment of subtle changes in albumin concentration, the primary macromolecular component of urine, is critical for the diagnosis of early stage albuminuria, one of the major complications in nephropathy.
Human Serum Albumin Characterisation And Binding Studies By Spectroscopic Techniques
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Author : Beulah A. Banfield
language : en
Publisher:
Release Date : 2010
Human Serum Albumin Characterisation And Binding Studies By Spectroscopic Techniques written by Beulah A. Banfield and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2010 with Serum albumin categories.
Serum Albumin (HSA) is a plasma protein of great significance with an ability to bind nerous endogenous and exogenous ligands, having a single polypeptide chain of 585 amino constructed in three domains of relatively equal size. Although HSA's existence has been own for many years, its characterisation and ability to bind ligands still remain enigmatic. Only 11992 was the crystal structure of HSA reported (Carter and Ho, 1992). Effective crystallisation I the determination of meaningful crystallographic data and structure had proven difficult. The I report concerned HSA crystals grown using zero gravity conditions. i objective of this project is the characterisation of recombinant and native HSA using Ultra-Diet (UV) & circular dichroism spectroscopy (CD) and involved HSA conformational changes, hich altered the ability to bind or off-load ligands. Changing environment, together with the use F characteristic "marker ligands," influences binding to provide a handle that can be utilised and litored. This enables the assignment of binding sites and the study of perturbating conditions. jing conditions such as pH, temperature, ionic strength and solvents in the presence and of ligands were employed to extract further information on this elusive protein, tients of recombinant HSA were also used (namely domain I and domain I + II) under tical conditions as the whole protein in order to help elucidate and assign binding sites.
Albumin Structure Function And Uses
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Author : Victor M. Rosenoer
language : en
Publisher: Elsevier
Release Date : 2014-05-18
Albumin Structure Function And Uses written by Victor M. Rosenoer and has been published by Elsevier this book supported file pdf, txt, epub, kindle and other format this book has been release on 2014-05-18 with Medical categories.
Albumin Structure, Function and Uses reviews the many facets of serum albumin, including its history and evolutionary development, structure and function, synthesis, degradation, distribution and transport, and metabolic behavior. The use, misuse, and abuse of albumin in the treatment of disease are also discussed. This book is comprised of 17 chapters and begins with a commentary on how albumin is used, misused, and abused in the treatment of disease such as peptic ulcer, and a description of the real indications for its use. Concepts in albumin purification are then examined, along with the amino acid sequence of serum albumin and some aspects of its structure and conformational properties. Subsequent chapters explore the phylogenetics of albumin; albumin binding sites; clinical implications of drug-albumin interaction; genetics of human serum albumin; and hepatic synthesis of export proteins. Albumin catabolism and intracellular transport are also considered, together with surgical and clinical aspects of albumin metabolism. This monograph should be a useful resource for biochemists and clinicians.
Combining Docking And Molecular Dynamic Analysis To Probe Human Serum Albumin Cucurbitacin E Interaction
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Author : Elia Rabih
language : fr
Publisher:
Release Date : 2011
Combining Docking And Molecular Dynamic Analysis To Probe Human Serum Albumin Cucurbitacin E Interaction written by Elia Rabih and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2011 with categories.
Constructing Genetic And Chemical Variants Of Human Serum Albumin Reconstituted With Heme And Testing For Nitrite Reductase Activity
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Author : Alexandra Alfonso Castro
language : en
Publisher:
Release Date : 2018
Constructing Genetic And Chemical Variants Of Human Serum Albumin Reconstituted With Heme And Testing For Nitrite Reductase Activity written by Alexandra Alfonso Castro and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2018 with categories.
Human serum albumin (HSA) is abundantly present in our blood and is a repository to many molecules, such as heme. Previous studies have confirmed that HSA reconstituted with heme (HSA-heme) imitates the binding site of other heme enzymes such as myoglobin (Mb) and hemoglobin (Hb), except that an O(tyrosine) bonds to the Fe center of heme instead of a N(histidine) that is present in Mb and Hb. Although the primary function of Mb and Hb is to store and carry oxygen in the muscles and blood, respectively, they also have a secondary function of producing nitric oxide through the reduction of nitrite under hypoxic conditions. The aim of this project is to obtain imidazole complexes of HSA reconstituted with heme (HSA-hemeIm), and then test for their nitrite reductase (NiR) activity. This can be achieved by titrating the protein with imidazole compounds, specifically imidazole (Im), 1-methylimidazole (1-Im), and 2-methylimidazole (2-Im). Adding imidazole to HSA-heme may cause the formation of a N(imidazole) bond to Fe, providing a system that mimics the active site of Mb and Hb. HSA-heme is complexed with an imidazole derivative and reacted with nitrite. This reaction is monitored with UV-Vis spectroscopy. The spectrum is compared to that of HSA-heme imidazole derivative reacted with nitric oxide. These two spectra are very similar, indicating that HSA-hemeIm converts the nitrite into nitric oxide. Finally, the bimolecular rate constant obtained from the reaction between HSA-heme1-Im and nitrite is smaller than that obtained for the respective NiR reaction of wild-type (wt) HSA-heme or Mb.
Design Of Selective Ligands For Conjugate Drug Targeting To Human Serum Albumin Hsa Through Cysteine 34 And Beta D Galactopyranoside Inhibitors Towards Galectins
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Author : Subhash Rao Rauthu
language : en
Publisher:
Release Date : 2011
Design Of Selective Ligands For Conjugate Drug Targeting To Human Serum Albumin Hsa Through Cysteine 34 And Beta D Galactopyranoside Inhibitors Towards Galectins written by Subhash Rao Rauthu and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2011 with categories.