TY - JOUR
T1 - Interactions of cationic gold nanoclusters with serum proteins and effects on their cellular responses
AU - Wen, Mengyao
AU - Li, Yixiao
AU - Zhong, Wencheng
AU - Li, Qingfang
AU - Cao, Liping
AU - Tan, Li li
AU - Shang, Li
N1 - Publisher Copyright:
© 2021 Elsevier Inc.
PY - 2022/3/15
Y1 - 2022/3/15
N2 - Cationic nanoparticles (NPs) have shown great potential in biological applications owing to their distinct features such as favorable cellular internalization and easy binding to biomolecules. However, our current knowledge of cationic NPs’ biological behavior, i.e., NP–protein interactions, is still rather limited. Herein, we choose ultrasmall-sized fluorescent gold nanoclusters (AuNCs) coated by (11-mercaptoundecyl) - N, N, N - trimethylammonium bromide (MUTAB) as representative cationic NPs, and systematically study their interactions with different serum proteins at nano-bio interfaces. By monitoring the fluorescence intensity of MUTAB-AuNCs, all proteins are observed to bind with roughly micromolar affinities to AuNCs and quench their fluorescence. Transient fluorescence spectroscopy, X-ray photoelectron spectroscopy and isothermal titration calorimetry are also adopted to characterize the physicochemical properties of MUTAB-AuNCs after the protein adsorption. Concomitantly, circular dichroism spectroscopy reveals that cationic AuNCs can exert protein-dependent conformational changes of these serum proteins. Moreover, protein adsorption onto cationic AuNCs can significantly influence their cellular responses such as cytotoxicity and uptake efficiency. These results provide important knowledge towards understanding the biological behaviors of cationic nanoparticles, which will be helpful in further designing and utilizing them for safe and efficient biomedical applications.
AB - Cationic nanoparticles (NPs) have shown great potential in biological applications owing to their distinct features such as favorable cellular internalization and easy binding to biomolecules. However, our current knowledge of cationic NPs’ biological behavior, i.e., NP–protein interactions, is still rather limited. Herein, we choose ultrasmall-sized fluorescent gold nanoclusters (AuNCs) coated by (11-mercaptoundecyl) - N, N, N - trimethylammonium bromide (MUTAB) as representative cationic NPs, and systematically study their interactions with different serum proteins at nano-bio interfaces. By monitoring the fluorescence intensity of MUTAB-AuNCs, all proteins are observed to bind with roughly micromolar affinities to AuNCs and quench their fluorescence. Transient fluorescence spectroscopy, X-ray photoelectron spectroscopy and isothermal titration calorimetry are also adopted to characterize the physicochemical properties of MUTAB-AuNCs after the protein adsorption. Concomitantly, circular dichroism spectroscopy reveals that cationic AuNCs can exert protein-dependent conformational changes of these serum proteins. Moreover, protein adsorption onto cationic AuNCs can significantly influence their cellular responses such as cytotoxicity and uptake efficiency. These results provide important knowledge towards understanding the biological behaviors of cationic nanoparticles, which will be helpful in further designing and utilizing them for safe and efficient biomedical applications.
KW - Cationic nanoparticles
KW - Cellular uptake
KW - Fluorescence
KW - Gold nanoclusters
KW - Protein adsorption
UR - http://www.scopus.com/inward/record.url?scp=85121108284&partnerID=8YFLogxK
U2 - 10.1016/j.jcis.2021.12.044
DO - 10.1016/j.jcis.2021.12.044
M3 - 文章
C2 - 34922069
AN - SCOPUS:85121108284
SN - 0021-9797
VL - 610
SP - 116
EP - 125
JO - Journal of Colloid and Interface Science
JF - Journal of Colloid and Interface Science
ER -