Understanding protein/gold nanoparticle (AuNP) interaction holds key to a wide range of protein and AuNP applications that include biosensing, AuNP based drug delivery and cancer therapy.  It is known that protein can spontaneously assemble onto the AuNP surface, forming a protein coating layer commonly refered to �protein corona�.  Recent study from our group indicates that protein corona formed by bovine serum albumin (BSA) is highly permeable and a large fraction of the protein covered AuNP surface can be made available for further organothiols adsorption without compromising stability (with no detachement) of the protein coating layer.   Present here is an UV-vis, NMR, and surface enhancement Raman spectroscopic study of stability of the thrid IgG-binding domain of Protein G (GB3) covered AuNP where the cysteine content is systematically varied.   Three organothiols that differ in their thiol and amine contents are employed as the molecular probes to study the correlation between the stability of GB3 on AuNP and the cysteine content.

Understanding the protein binding with gold nanoparticle using organothiol as molecular probes

244th National Meeting (2012)

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