36
views
0
recommends
+1 Recommend
1 collections
    0
    shares

      To submit to Bentham Journals, please click here

      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Viscosity Control of Protein Solution by Small Solutes: A Review

      review-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Viscosity of protein solution is one of the most troublesome issues for the high-concentration formulation of protein drugs. In this review, we summarize the practical methods that suppress the viscosi-ty of protein solution using small molecular additives. The small amount of salts decreases the viscosity that results from electrostatic repulsion and attraction. The chaotrope suppresses the hydrophobic attraction and cluster formation, which can lower the solution viscosity. Arginine hydrochloride (ArgHCl) also sup-presses the solution viscosity due to the hydrophobic and aromatic interactions between protein molecules. The small molecular additives are the simplest resolution of the high viscosity of protein solution as well as understanding of the primary cause in complex phenomena of protein interactions.

          Related collections

          Most cited references103

          • Record: found
          • Abstract: found
          • Article: not found

          Overcoming the challenges in administering biopharmaceuticals: formulation and delivery strategies.

          The formulation and delivery of biopharmaceutical drugs, such as monoclonal antibodies and recombinant proteins, poses substantial challenges owing to their large size and susceptibility to degradation. In this Review we highlight recent advances in formulation and delivery strategies--such as the use of microsphere-based controlled-release technologies, protein modification methods that make use of polyethylene glycol and other polymers, and genetic manipulation of biopharmaceutical drugs--and discuss their advantages and limitations. We also highlight current and emerging delivery routes that provide an alternative to injection, including transdermal, oral and pulmonary delivery routes. In addition, the potential of targeted and intracellular protein delivery is discussed.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Interactions between macromolecules and ions: The Hofmeister series.

            The Hofmeister series, first noted in 1888, ranks the relative influence of ions on the physical behavior of a wide variety of aqueous processes ranging from colloidal assembly to protein folding. Originally, it was thought that an ion's influence on macromolecular properties was caused at least in part by 'making' or 'breaking' bulk water structure. Recent time-resolved and thermodynamic studies of water molecules in salt solutions, however, demonstrate that bulk water structure is not central to the Hofmeister effect. Instead, models are being developed that depend upon direct ion-macromolecule interactions as well as interactions with water molecules in the first hydration shell of the macromolecule.
              Bookmark
              • Record: found
              • Abstract: not found
              • Article: not found

              Effect of ions on the structure of water: structure making and breaking.

                Bookmark

                Author and article information

                Journal
                Curr Protein Pept Sci
                Curr. Protein Pept. Sci
                CPPS
                Current Protein & Peptide Science
                Bentham Science Publishers
                1389-2037
                1875-5550
                September 2018
                September 2018
                : 19
                : 8
                : 746-758
                Affiliations
                [1]Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8573 , Japan
                Author notes
                [* ]Address correspondence to this author at the Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan; Tel/Fax +81-29-853-5306; E-mail: shiraki@ 123456bk.tsukuba.ac.jp
                Article
                CPPS-19-746
                10.2174/1389203719666171213114919
                6182935
                29237380
                513dd7fa-585f-4c12-a986-3d581a9e04d4
                © 2018 Bentham Science Publishers

                This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) ( https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

                History
                : 27 September 2017
                : 01 December 2017
                : 02 December 2017
                Categories
                Article

                Biochemistry
                viscosity,arginine,antibody,immunoglobulin g,protein aggregation,serum albumin,molecular interaction

                Comments

                Comment on this article