Tannic acid as a precipitating agent of human plasma proteins

The search for plasma proteins precipitation methods has been increasing due to the plasma protein therapeutic needs in world-wide. Thus, this work evaluates the tannic acid (TA) ability to precipitate proteins from human plasma. In this study, TA-plasma protein complexes were studied at different p...

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Bibliographic Details
Published in:European journal of pharmaceutical sciences 2019-10, Vol.138, p.105018-105018, Article 105018
Main Authors: Pinto, Aline Ferreira, Nascimento, Jéssica Miranda do, Sobral, Renata Vitória da Silva, Amorim, Elba Lúcia Cavalcanti de, Silva, Ricardo Oliveira, Leite, Ana Cristina Lima
Format: Article
Language:English
Subjects:
Albumin
Circular Dichroism - methods
Human plasma
Humans
Immunoglobulin G
Mass Spectrometry - methods
Particle Size
Plasma - chemistry
Plasma proteins
Protein precipitation
Serum Albumin, Human - chemistry
Serum Globulins - chemistry
Tannic acid
Tannins - chemistry
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Summary:The search for plasma proteins precipitation methods has been increasing due to the plasma protein therapeutic needs in world-wide. Thus, this work evaluates the tannic acid (TA) ability to precipitate proteins from human plasma. In this study, TA-plasma protein complexes were studied at different pH conditions, tannin/plasma ratio and reaction mixing time. The complexes formed from combinations of TA and plasma proteins were analyzed by gel electrophoresis, protein quantification, particle size, charge, mass spectrometry, microscopic image, and circular dichroism. It was possible to verify the precipitate formation in all tested pH values, with high precipitation at pH 5. The native PAGE analysis showed three mainly bands corresponding independent of the pHs used. It was possible to observe a gradual growing of precipitate protein in the first precipitation process (P1) when increased the TA/plasma ratio. 15 min of incubation was enough to precipitate 72.3% of proteins. Spectroscopic analyzes showed albumin signals and the electron microscopy analysis of IgG-TA confirmed the compact form of a precipitate. According to CD, formation of the IgG-TA complexes does not cause a major structural change of the protein. From the results obtained, it was possible to establish some parameters for plasma proteins precipitation using TA. [Display omitted]
ISSN:0928-0987
1879-0720
DOI:10.1016/j.ejps.2019.105018