Low cetyltrimethylammonium bromide concentrations induce reversible amorphous aggregation of tobacco mosaic virus and its coat protein at room temperature

Panyukov, Yuliy V.; Nemykh, Maria A.; Rafikova, E. R.; Bi, Kurganov; Yaguzhinsky, L. S.; Arutyunyan, Alexander M.; Drachev, V. A.; Добров, Е. Н.

doi:10.1016/j.biocel.2005.10.014

Cited by 9 publications

(22 citation statements)

References 46 publications

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“…It was observed that the rate of the light scattering intensity increase in the course of CTAB-induced amorphous aggregation rises with the increase in the [CTAB]:[CP] ratio (Fig. 7A) and closely follows the turbidity (A 320 ) changes [14]. At the same time the kinetics of the R h change (Fig.…”

Section: Dls Study Of Kinetics Of Ctab-induced Tmv Cp Amorphous Aggrementioning

confidence: 89%

“…In contrast to the thermal TMV CP aggregation, the CTAB-induced aggregation occurred without any visible changes in the protein structure [14]. Therefore, we decided to study CTAB-induced amorphous aggregation of TMV CP using DLS.…”

Section: Dls Study Of Kinetics Of Ctab-induced Tmv Cp Amorphous Aggrementioning

confidence: 97%

“…Recently we have observed that the TMV CP amorphous aggregation can be also induced in neutral phosphate buffer (PB) at room temperature (25°C) by low micromolar concentrations of cationic surfactant cetyltrimethylammonium bromide (CTAB) [14].…”

Section: Introductionmentioning

confidence: 99%

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The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering

Panyukov

Yudin

Drachev

et al. 2007

Biophysical Chemistry

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Section: Dls Study Of Kinetics Of Ctab-induced Tmv Cp Amorphous Aggrementioning

confidence: 89%

Section: Dls Study Of Kinetics Of Ctab-induced Tmv Cp Amorphous Aggrementioning

confidence: 97%

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The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering

Panyukov

Yudin

Drachev

et al. 2007

Biophysical Chemistry

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“…Cationic surfactant cetyltrimethylammonium bromide (CTAB) was shown to bind the subunit of the tobacco mosaic virus coat protein in a 4:1 molar ratio, and binding does seem to alter the native structure of the protein. 234 Like nonionic surfactants, the binding between the nonpolar chain/structure of ionic surfactants and protein may shield the nonspecifi c interactions between protein hydrophobic patches/groups. In addition, the high charge density of ionic surfactants on the protein surface could possibly induce a charge -screening effect between the protein polar groups.…”

Section: Ionic Surfactantsmentioning

confidence: 99%

“…CTAB at low micromolar concentrations (start at about 15 µ M) induced aggregation of tobacco mosaic virus coat protein at 25 ° C, but no aggregation was observed at higher surfactant concentrations (above 300 µ M). 234 …”

Section: Ionic Surfactantsmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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Protein and Peptide Formulation Development

Ohtake¹,

Wang²

2013

Pharmaceutical Sciences Encyclopedia

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Proteins/peptides are generally much more sensitive to process‐ or storage‐induced degradations than small synthetic molecules. Therefore, significant efforts are needed to formulate these protein/peptide drug candidates into viable commercial products.This chapter reviews the degradation processes in proteins/peptides, describes factors affecting protein/peptide stability, and discusses strategies in the successful development and manufacturing of protein/peptide commercial products.

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Low cetyltrimethylammonium bromide concentrations induce reversible amorphous aggregation of tobacco mosaic virus and its coat protein at room temperature

Cited by 9 publications

References 46 publications

The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering

The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering

External Factors Affecting Protein Aggregation

Protein and Peptide Formulation Development

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