engleski

Protein self-association

Monomeric protein structure can form dimers, trimers and other aggregates induced by different types of stressors. During protein association process different types of bonding may occur, such as covalent, especially disulfide bonds, and non- covalent bonds: hydrogen bonds, electrostatic interactions, Van der Waals interactions and hydrophobic bonds. Protein structure complexity makes mechanism of aggregates emergence entirely unrevealed or poorly described. Affected by these stressors, covalent and non- covalent bondage may occur and produce irreversible or reversible protein aggregates. Irreversible aggregates can be produced through heating, freezing-thawing, over- concentrating, isomerization, oxidation, etc. On the other hand, reversible aggregates or self- associates might be formed by the aforementioned processes but most likely by agitation.1 We examined the formation of dimers, trimers, and tetramers on rHuG-CSG, also known as Granulocyte Colony Stimulating Factor, induced by agitation through a time period of 150 s. The analysis was performed immediately after agitation by liquid chromatography (gel permeation) at pH= 7.0 (50 mM NH4HCO3 mobile phase). Due to increased pressure caused by centripetal acceleration during agitation monomeric structures merges and makes dimers, trimers, tetramers, and other aggregates. Increased agitation power results in a significant increase of reversible self-associate quantity.

protein aggregates ; agitation ; rHuG-CSF ; filgrastim

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