Literature DB >> 23319172

Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: influence of colloidal and conformational stabilities.

Shuntaro Saito1, Jun Hasegawa, Naoki Kobayashi, Toshiaki Tomitsuka, Susumu Uchiyama, Kiichi Fukui.   

Abstract

PURPOSE: To develop a general strategy for optimizing monoclonal antibody (MAb) formulations.
METHODS: Colloidal stabilities of four representative MAbs solutions were assessed based on the second virial coefficient (B 2) at 20°C and 40°C, and net charges at different NaCl concentrations, and/or in the presence of sugars. Conformational stabilities were evaluated from the unfolding temperatures. The aggregation propensities were determined at 40°C and after freeze-thawing. The electrostatic potential of antibody surfaces was simulated for the development of rational formulations.
RESULTS: Similar B 2 values were obtained at 20°C and 40°C, implying little dependence on temperature. B 2 correlated quantitatively with aggregation propensities at 40°C. The net charge partly correlated with colloidal stability. Salts stabilized or destabilized MAbs, depending on repulsive or attractive interactions. Sugars improved the aggregation propensity under freeze-thaw stress through improved conformational stability. Uneven and even distributions of potential surfaces were attributed to attractive and strong repulsive electrostatic interactions.
CONCLUSIONS: Assessment of colloidal stability at the lowest ionic strength is particularly effective for the development of formulations. If necessary, salts are added to enhance the colloidal stability. Sugars further improved aggregation propensities by enhancing conformational stability. These behaviors are rationally predictable according to the surface potentials of MAbs.

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Year:  2013        PMID: 23319172     DOI: 10.1007/s11095-012-0965-4

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


  56 in total

1.  The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein.

Authors:  A W Vermeer; W Norde
Journal:  Biophys J       Date:  2000-01       Impact factor: 4.033

2.  Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor.

Authors:  Eva Y Chi; Sampathkumar Krishnan; Brent S Kendrick; Byeong S Chang; John F Carpenter; Theodore W Randolph
Journal:  Protein Sci       Date:  2003-05       Impact factor: 6.725

Review 3.  Colloidal behavior of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution.

Authors:  Joseph J Valente; Robert W Payne; Mark Cornell Manning; W William Wilson; Charles S Henry
Journal:  Curr Pharm Biotechnol       Date:  2005-12       Impact factor: 2.837

4.  Molecular origins of osmotic second virial coefficients of proteins.

Authors:  B L Neal; D Asthagiri; A M Lenhoff
Journal:  Biophys J       Date:  1998-11       Impact factor: 4.033

5.  Behavior of monoclonal antibodies: relation between the second virial coefficient (B (2)) at low concentrations and aggregation propensity and viscosity at high concentrations.

Authors:  Shuntaro Saito; Jun Hasegawa; Naoki Kobayashi; Naoyuki Kishi; Susumu Uchiyama; Kiichi Fukui
Journal:  Pharm Res       Date:  2011-08-19       Impact factor: 4.200

6.  Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange.

Authors:  Aming Zhang; Satish K Singh; Michael R Shirts; Sandeep Kumar; Erik J Fernandez
Journal:  Pharm Res       Date:  2011-07-30       Impact factor: 4.200

7.  Surface-induced denaturation of proteins during freezing and its inhibition by surfactants.

Authors:  B S Chang; B S Kendrick; J F Carpenter
Journal:  J Pharm Sci       Date:  1996-12       Impact factor: 3.534

8.  Effect of mannitol crystallinity on the stabilization of enzymes during freeze-drying.

Authors:  K Izutsu; S Yoshioka; T Terao
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9.  Excipients differentially influence the conformational stability and pretransition dynamics of two IgG1 monoclonal antibodies.

Authors:  Santosh V Thakkar; Sangeeta B Joshi; Matthew E Jones; Hasige A Sathish; Steven M Bishop; David B Volkin; C Russell Middaugh
Journal:  J Pharm Sci       Date:  2012-05-11       Impact factor: 3.534

10.  Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions.

Authors:  Donald J Winzor; Marcin Deszczynski; Stephen E Harding; Peter R Wills
Journal:  Biophys Chem       Date:  2007-03-07       Impact factor: 2.352

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  11 in total

1.  Assessment of the Protein-Protein Interactions in a Highly Concentrated Antibody Solution by Using Raman Spectroscopy.

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Journal:  Pharm Res       Date:  2015-12-16       Impact factor: 4.200

2.  Bilateral Effects of Excipients on Protein Stability: Preferential Interaction Type of Excipient and Surface Aromatic Hydrophobicity of Protein.

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Review 3.  High-throughput biophysical analysis of protein therapeutics to examine interrelationships between aggregate formation and conformational stability.

Authors:  Rajoshi Chaudhuri; Yuan Cheng; C Russell Middaugh; David B Volkin
Journal:  AAPS J       Date:  2013-10-31       Impact factor: 4.009

Review 4.  Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.

Authors:  Allen P Minton
Journal:  Anal Biochem       Date:  2016-02-17       Impact factor: 3.365

5.  Direct analysis of mAb aggregates in mammalian cell culture supernatant.

Authors:  Albert J Paul; Karen Schwab; Friedemann Hesse
Journal:  BMC Biotechnol       Date:  2014-11-29       Impact factor: 2.563

6.  Characterizing monoclonal antibody formulations in arginine glutamate solutions using 1H NMR spectroscopy.

Authors:  Priscilla Kheddo; Matthew J Cliff; Shahid Uddin; Christopher F van der Walle; Alexander P Golovanov
Journal:  MAbs       Date:  2016-08-11       Impact factor: 5.857

7.  Characterizing and Minimizing Aggregation and Particle Formation of Three Recombinant Fusion-Protein Bulk Antigens for Use in a Candidate Trivalent Rotavirus Vaccine.

Authors:  Sanjeev Agarwal; Neha Sahni; John M Hickey; George A Robertson; Robert Sitrin; Stanley Cryz; Sangeeta B Joshi; David B Volkin
Journal:  J Pharm Sci       Date:  2019-08-07       Impact factor: 3.534

8.  The effect of arginine glutamate on the stability of monoclonal antibodies in solution.

Authors:  Priscilla Kheddo; Malgorzata Tracka; Jonathan Armer; Rebecca J Dearman; Shahid Uddin; Christopher F van der Walle; Alexander P Golovanov
Journal:  Int J Pharm       Date:  2014-06-30       Impact factor: 5.875

9.  R409K mutation prevents acid-induced aggregation of human IgG4.

Authors:  Hiroshi Namisaki; Seiji Saito; Keiko Hiraishi; Tomoko Haba; Yoshitaka Tanaka; Hideaki Yoshida; Shigeru Iida; Nobuaki Takahashi
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10.  Mitigation of liquid-liquid phase separation of a monoclonal antibody by mutations of negative charges on the Fab surface.

Authors:  Tatsuji Matsuoka; Ryuki Miyauchi; Nobumi Nagaoka; Jun Hasegawa
Journal:  PLoS One       Date:  2020-10-30       Impact factor: 3.240

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