When not in their natural biological environments, proteins are often unstable which can result in a loss of activity and / or aggregation. Optimal conditions for storage must be found and since proteins are an extremely heterogeneous class of molecules the range of buffer conditions necessary can vary widely for each protein.

Often common conditions include screening a small range of compounds (e.g. reducing agents and detergents) for storage at 4ºC, using glycerol or PEG together with freeze/thawing and lyophilisation – specific conditions can then be found and employed for individual proteins but there are disadvantages associated with each method.

NVoy technology can stabilise proteins due to the inherent characteristics of our NV molecules. They are linear, uncharged polymers which have been specifically derivatised to present a highly hydrophobic face yet remain highly soluble. The hydrophobic parts of the molecules associating with proteins at multiple points to stop aggregation occurring. Association with proteins is dynamic and the molecules can be used at low concentrations relative to the protein. Their size (Hydrodynamic Radius c.a. 18 kDa) prevents them from entering the proteins core and thus inhibiting normal structural bonding or blocking catalytic / binding sites.

Since the NVoy associates with any surface exposed hydrophobicity and prevents aggregation in the vast majority of cases, it offers a generic solution allowing proteins to be held in a soluble and stable form for longer.  In addition, NVoy will help reduce any problems assaociated with non-specific binding of your target protein to contaminant proteins or process surfaces (i.e. purification resins / filtration membranes).

For further information please contact us at: info@expedeon.com