AUC 2022

View Contributions

Insights into Protein-Stabilized Gold Nanoclusters from Multi-Wavelength Analytical Ultracentrifugation
Submitter: Ozlem Akyuz
Authors: Özlem Akyüz, Rose Rosenberg, Maite Mißun, Andreas Marx, Helmut Cölfen
Corresponding Author: Özlem Akyüz
Title: Insights into Protein-Stabilized Gold Nanoclusters from Multi-Wavelength Analytical Ultracentrifugation
Contribution Type: Full Talk
Selected for Presentation Yes
Abstract: Gold nanoclusters (AuNC) are ultra small-sized entities (<3 nm)[1] exhibiting molecular-like electronic properties[2] and having intrinsic catalytic activity[3]. Characteristics of the stabilizing ligand of AuNC are critical because of the fact that they change the photoluminescence and catalytic properties of the AuNC by influencing the electron transfer mechanisms[4] and size distributions[5]. Proteins have been widely chosen as stabilizing ligands to maintain the biocompatibility and functionality of the AuNC in biological applications[6]. However, protein surface charge and folding are affected during the synthesis of AuNC via the bio-friendly synthesis route[7]. Therefore, it is pivotal to investigate the hydrodynamic properties of the protein-stabilized AuNC in real environmental conditions for further understanding of the biological activity and catalytic performance of the protein-stabilized AuNC.
Herein, we employed Multi-Wavelength Analytical Ultracentrifugation (MWL-AUC)[8] to reveal the molecular mass, shape factor, and hydration degree of bovine serum albumin (BSA) stabilized AuNC (AuNC@BSA) and genetically cysteine engineered Klentaq DNA Polymerase (KTQ5C) stabilized AuNC (AuNC@KTQ5C). Thereby, we had detailed insights into structural properties, enzymatic performance, and size of the protein-stabilized AuNC.

[1] A. Yahia-Ammar, D. Sierra, F. Merola, N. Hildebrandt, X. Le Guevel, ACS Nano 2016, 10, 2591-2599.
[2] M. Zhu, C. M. Aikens, F. J. Hollander, G. C. Schatz, R. Jin, J. Am. Chem. Soc 2008, 130, 5883–5885.
[3] C. N. Loynachan, A. P. Soleimany, J. S. Dudani, Y. Lin, A. Najer, A. Bekdemir, Q. Chen, S. N. Bhatia, M. M. Stevens, Nat Nanotechnol 2019, 14, 883-890.
[4] Z. Wu, R. Jin, Nano Lett 2010, 10, 2568-2573.
[5] Y. Xu, J. Sherwood, Y. Qin, D. Crowley, M. Bonizzoni, Y. Bao, Nanoscale 2014, 6, 1515-1524.
[6] A. Cifuentes-Rius, V. G. Deepagan, J. Xie, N. H. Voelcker, ACS Appl Mater Interfaces 2021, 13, 49581-49588.
[7] K. Chaudhari, P. L. Xavier, T. Pradeep, ACS Nano 2011, 5, 8816-8827.
[8] J. Z. Pearson, F. Krause, D. Haffke, B. Demeler, K. Schilling, H. Cölfen, Methods Enzymol 2015, 562, 1-26.