Polyallylamine hydrochloride coating enhances the fluorescence emission of human serum albumin encapsulated gold nanoclusters

Russell, Ben Allan and Jachimska, Barbara and Chen, Yu (2018) Polyallylamine hydrochloride coating enhances the fluorescence emission of human serum albumin encapsulated gold nanoclusters. Journal of Photochemistry and Photobiology B: Biology, 187. pp. 131-135. ISSN 1011-1344

[thumbnail of Russell-etal-JOPPB-2018-Polyallylamine-hydrochloride-coating-enhances-the-fluorescence-emission-of-human]
Text (Russell-etal-JOPPB-2018-Polyallylamine-hydrochloride-coating-enhances-the-fluorescence-emission-of-human)
Accepted Author Manuscript
License: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 logo

Download (770kB)| Preview


    Protein encapsulated gold nanoclusters have received much attention due to the possibility of using them as a non-toxic fluorescent probe or marker for biomedical applications, however one major disadvantage currently is their low brightness and quantum yield in comparison to currently used fluorescent markers. A method of increasing the fluorescence emission of Human Serum Albumin (HSA) encapsulated gold nanoclusters (AuNCs) via a Polyallylamide hydrochloride (PAH) coating is described. PAH molecules with a molecular weight of ~17,500 Da were found to enhance the fluorescence emission of HSA-AuNCs by 3-fold when the protein/polymer concentration ratio is 2:1 in solution. Interestingly, the fluorescence lifetime of the AuNCs was found to decrease while the native tryptophan (TRP) fluorescence lifetime also decreased during the fluorescence emission intensity enhancement caused by the PAH binding. Coinciding with the decrease in fluorescence lifetime, the zeta potential of the system was observed to be zero during maximum fluorescence intensity enhancement, causing the formation of large aggregates. These results suggest that PAH binds to the HSA-AuNCs acting as a linker; causing aggregation and rigidification, which results in a decrease in separation between native TRP of HSA and AuNCs; improving Förster Resonance Energy Transfer (FRET) and increasing the fluorescence emission intensity. These findings are critical to the development of brighter protein encapsulated AuNCs.

    ORCID iDs

    Russell, Ben Allan ORCID logoORCID: https://orcid.org/0000-0002-8740-6040, Jachimska, Barbara and Chen, Yu;