Conformational stability as a quality attribute for the cell therapy raw material human serum albumin

Wynendaele, Evelien; Junren, Gamaliel; Xu, Xiaolong; Cho, Nam‐Joon; Spiegeleer, Bart De

doi:10.1039/d1ra01064f

Cited by 5 publications

(4 citation statements)

References 54 publications

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“…[108] Whereas recombinant HSA containing octanoate stabilizer disclosed maximum solution-phase conformational stability and minimum adsorption-related deformation among all tested albumin samples. [109] By contrast, adsorption studies demonstrate least conformational stability was observed by BSA derived from plasma compared to other tested samples and underwent colloidal stability and conformational changes upon exposure to external stresses such as solid-liquid interfaces and high temperature. [108,109] For drug binding and conjugation, HSA shows superiority owing to the hollow cavity of subdomain II.…”

Section: Hsa Bsamentioning

confidence: 93%

“…[109] By contrast, adsorption studies demonstrate least conformational stability was observed by BSA derived from plasma compared to other tested samples and underwent colloidal stability and conformational changes upon exposure to external stresses such as solid-liquid interfaces and high temperature. [108,109] For drug binding and conjugation, HSA shows superiority owing to the hollow cavity of subdomain II. [110] BSA employed Leu-237 residue on subdomain IIA directed toward the least carrying capability.…”

Section: Hsa Bsamentioning

confidence: 93%

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Electrospinning of bovine serum albumin‐based nano‐fibers: From synthesis to medical prospects; Challenges and future directions

Hayat,

Bukhari,

Irfan

2023

Biotechnology Journal

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Bovine serum albumin (BSA) is a globular non‐glycoprotein that has gotten a lot of attention because of its unique properties like biocompatibility, biodegradability, non‐immunogenicity, non‐toxicity, and strong resemblance to the natural extracellular matrix (ECM). Given its robust mechanical properties, such as interfacial tension, conductivity, swelling resistance, and viscoelasticity, it can be concluded that it is an appropriate matrix for producing novel BSA‐based nanoconstructs. Thus, simple analytic methods are required for accurately detecting BSA as a model protein in medical sciences and healthcare. Furthermore, the characteristics mentioned above aid BSA in the electrospinning process, which results in fibres conjugated with other polymers. Electrospun synthesis has recently received much attention for its ability to produce stable, biomimicking, highly porous, 3D BSA‐derived nano‐fibers. As a result, BSA‐based nano‐fibers have achieved exclusive developments in the medical sector, such as tissue engineering for the remodelling of damaged tissue or organ repair by creating artificial ones.Meanwhile, they could be used as drug delivery systems for target‐specific drug delivery, wound dressings, etc. This study illustrates the structural and physicochemical properties of BSA and the determination of BSA using various methods, by citing recent reports and current developments in the medical field. Furthermore, current challenges and future directions are also highlighted.This article is protected by copyright. All rights reserved

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Section: Hsa Bsamentioning

confidence: 93%

Section: Hsa Bsamentioning

confidence: 93%

Electrospinning of bovine serum albumin‐based nano‐fibers: From synthesis to medical prospects; Challenges and future directions

Hayat,

Bukhari,

Irfan

2023

Biotechnology Journal

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“…This means that HSA molecules are more prone to aggregating or sticking together in solution, which can lead to a loss in stability and an increase in solution viscosity. On the other hand, BSA has higher colloidal stability, meaning that its molecules are more resistant to aggregation and precipitation, resulting in a more stable and uniform solution structure [54]. Overall, the difference in stiffness between the HSA and BSA solutions could be attributed to their structural differences and resulting differences in binding forces, as well as their conformational and colloidal stabilities.…”

Section: Brillouin Scattering Of Bsa and Hsa Solutionsmentioning

confidence: 99%

Mechano-Chemistry across Phase Transitions in Heated Albumin Protein Solutions

et al. 2023

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The presence of certain proteins in biofluids such as synovial fluid, blood plasma, and saliva gives these fluids non-Newtonian viscoelastic properties. The amount of these protein macromolecules in biofluids is an important biomarker for the diagnosis of various health conditions, including Alzheimer’s disease, cardiovascular disorders, and joint quality. However, existing technologies for measuring the behavior of macromolecules in biofluids have limitations, such as long turnaround times, complex protocols, and insufficient sensitivity. To address these issues, we propose non-contact, optical Brillouin and Raman spectroscopy to assess the viscoelasticity and chemistry of non-Newtonian solutions, respectively, at different temperatures in several minutes. In this work, bovine and human serum albumin solution-based biopolymers were studied to obtain both their collective dynamics and molecular chemical evolution across heat-driven phase transitions at various protein concentrations. The observed phase transitions at elevated temperatures could be fully delayed in heated biopolymers by appropriately raising the level of protein concentration. The non-contact optical monitoring of viscoelastic and chemical property evolution could represent novel potential mechano-chemical biomarkers for disease diagnosis and subsequent treatment applications, including hyperthermia.

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“…Human serum albumin (HSA) is a principal extracellular protein with a concentration of 40 mg•mL −1 or 0.6 mM in blood plasma and contains 50-60% of total plasma protein in humans [7,8]. Research showed that the distribution, free concentration, and metabolism of drugs can be considerably altered as a result of their binding to HSA [9][10][11]. If the affinity of the drug binding to HSA in the plasma is strong, the drug will be transported to the target tissue and cannot be dissociated from HSA.…”

Section: Introductionmentioning

confidence: 99%

PI3K/mTOR Dual Inhibitor Pictilisib Stably Binds to Site I of Human Serum Albumin as Observed by Computer Simulation, Multispectroscopic, and Microscopic Studies

Yang

Zhang

et al. 2022

Molecules

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Pictilisib (GDC-0941) is a well-known dual inhibitor of class I PI3K and mTOR and is presently undergoing phase 2 clinical trials for cancer treatment. The present work investigated the dynamic behaviors and interaction mechanism between GDC-0941 and human serum albumin (HSA). Molecular docking and MD trajectory analyses revealed that GDC-0941 bound to HSA and that the binding site was positioned in subdomain IIA at Sudlow’s site I of HSA. The fluorescence intensity of HSA was strongly quenched by GDC-0941, and results showed that the HSA–GDC-0941 interaction was a static process caused by ground-state complex formation. The association constant of the HSA–GDC-0941 complex was approximately 105 M−1, reflecting moderate affinity. Thermodynamic analysis conclusions were identical with MD simulation results, which revealed that van der Waals interactions were the vital forces involved in the binding process. CD, synchronous, and 3D fluorescence spectroscopic results revealed that GDC-0941 induced the structural change in HSA. Moreover, the conformational change of HSA affected its molecular sizes, as evidenced by AFM. This work provides a useful research strategy for exploring the interaction of GDC-0941 with HSA, thus helping in the understanding of the transport and delivery of dual inhibitors in the blood circulation system.

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Conformational stability as a quality attribute for the cell therapy raw material human serum albumin

Abstract: An overall attribute for the consistency in pharmaceutical quality of human serum albumin encompasses a global measure of conformational stability, as measured by CD, DLS, QCM-D or LSPR.

Cited by 5 publications

References 54 publications

Electrospinning of bovine serum albumin‐based nano‐fibers: From synthesis to medical prospects; Challenges and future directions

Electrospinning of bovine serum albumin‐based nano‐fibers: From synthesis to medical prospects; Challenges and future directions

Mechano-Chemistry across Phase Transitions in Heated Albumin Protein Solutions

PI3K/mTOR Dual Inhibitor Pictilisib Stably Binds to Site I of Human Serum Albumin as Observed by Computer Simulation, Multispectroscopic, and Microscopic Studies

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