Editing Refolding by Dialysis (section)

== <span style="box-sizing: border-box; font-weight: 700; transition: none 0s ease 0s !important;">Refolding additives</span> ==

Protein refolding from denatured proteins is influenced by several factors, including solubility of protein, removal of denaturant, and assistance of refolding additives. The addition of chemical additives has been frequently used to prevent protein aggregation. Chemical additives can have effects in the following aspects: stabilizing the natural structure of correct folded proteins, changing the stability of misfolded proteins, increasing the solubility of folding intermediates and un-folded molecules. Commonly used chemical additives are shown below:



Denaturants: urea and GdnHCl<br/>Amino acids: Gly, Ala, Pro, and Arginine<br/>Polymers: PEG and cyclodextrin<br/>Polyols: glycerol<br/>Alcohol: short-chain alcohols<br/>Salts: NaCl, KCl, MgCl2 and (NH4)2SO4<br/>Sugars: glucose, sucrose and trehalose<br/>Detergents: Triton X-100, CHAPS, SDS and CTAB Detergents with cycloamylose or cyclodextran<br/>Artificial chaperones: thioredoxin, disulfide bond isomerase<br/>Reducing/oxidizing reagents: DTT, cysteine/cystine and glutathione<br/>Non-detergent zwitterionic agents: Non-detergent sulfobetaines (NDSB)

Though different techniques have developed for the generation of correctly folded protein from solubilized inclusion bodies, there is no universal refolding recipe for any protein. Proteins folding in solution are affected by a number of physiochemical parameters including ionic strength, pH, temperature, oxidation state and protein concentration as well as the presence of hydrophobic, polar, chaotropic agents and other proteins. For any given protein, the best refolding conditions still have to be determined empirically. BiologicsCorp has rich experiences to solve problems of protein refolding in E.coli. After evaluation of target proteins' biochemical and the structural properties, BiologicsCorp can offer flexible mature solutions to solve problems of protein refolding.