Nanoparticles are a rapidly emerging field due to their potential applications in the direct delivery of drugs for effective treatment of patients. However, when nanoparticles enter the blood, they are immediately swarmed with the circulating proteins which can affect the ability of the nanoparticle to reach the intended destination as the immune system tries to remove it from the circulation. A potential way to combat this issue is to precoat the nanoparticle with albumin, a non-immunogenic serum protein which can mask the nanoparticle and help it evade the immune system. This project aimed to evaluate whether the binding properties of two similar serum albumins- human and bovine- to 20nm gold nanoparticles, are significantly different to each other and therefore determine which would be more appropriate to use in order to stabilise the nanoparticle for use in nanomedicine. Through the use of a protein depletion assay, the maximum amount of protein bound to the nanoparticle could be identified, as well as the use of UV-Vis spectroscopy to perform an extinction peak assay to determine the dissociation constant of the proteins and therefore the binding affinity of the proteins to the gold nanoparticles. These values were then statistically analysed to find both the dissociation constant and amount of protein bound to the nanoparticle were not significantly different. These findings implied that the binding properties of the proteins were not significantly different so either protein- or recombinant proteins of similar properties- may be useful to stabilise the nanoparticle using a preformed protein corona. However, this experiment does not make any observations on the toxicity or other harmful factors that may be different between the two proteins when associated with an in vivo environment, and hence further assays would have to be performed before judgement can be made on the interchangeability of the use of different serum albumins.
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