TY - JOUR
T1 - Ultrathin NiMn layered double hydroxide nanosheets with a superior peroxidase mimicking performance to natural HRP for disposable paper-based bioassays
AU - Sun, Yue
AU - Xu, Hai
AU - Wang, Lumin
AU - Yu, Chenyang
AU - Zhou, Jinyuan
AU - Chen, Qiang
AU - Sun, Gengzhi
AU - Huang, Wei
N1 - Publisher Copyright:
© The Royal Society of Chemistry 2021.
PY - 2021/1/28
Y1 - 2021/1/28
N2 - The major obstacle to developing nanozymes which are considered as promising alternatives to natural enzymes is their moderate performance, including poor affinity for substrates, low catalytic activity, and severe pH-dependence. To address these issues, herein, we synthesize ultrathin layered double hydroxide (LDH) nanosheets with a thickness of 1.4 nm and an average lateral size of 23 nm using a fast-precipitation method. Through the rational design of their compositions, it is found that NiMn LDHs exhibit the optimum peroxidase mimicking performance with excellent substrate affinity, high catalytic activity (a limit of detection (LOD) of 0.04 μM H2O2) and robustness in a wide pH range (from 2.6 to 9.0), which is superior to that of natural horseradish peroxidase (HRP). The main active centers are identified as Mn sites because of their strong Lewis acidity and low redox potential. Furthermore, a series of disposable paper bioassays based on NiMn LDH nanozymes are designed and used for the highly sensitive detection of H2O2and ascorbic acid (AA).
AB - The major obstacle to developing nanozymes which are considered as promising alternatives to natural enzymes is their moderate performance, including poor affinity for substrates, low catalytic activity, and severe pH-dependence. To address these issues, herein, we synthesize ultrathin layered double hydroxide (LDH) nanosheets with a thickness of 1.4 nm and an average lateral size of 23 nm using a fast-precipitation method. Through the rational design of their compositions, it is found that NiMn LDHs exhibit the optimum peroxidase mimicking performance with excellent substrate affinity, high catalytic activity (a limit of detection (LOD) of 0.04 μM H2O2) and robustness in a wide pH range (from 2.6 to 9.0), which is superior to that of natural horseradish peroxidase (HRP). The main active centers are identified as Mn sites because of their strong Lewis acidity and low redox potential. Furthermore, a series of disposable paper bioassays based on NiMn LDH nanozymes are designed and used for the highly sensitive detection of H2O2and ascorbic acid (AA).
UR - http://www.scopus.com/inward/record.url?scp=85100465790&partnerID=8YFLogxK
U2 - 10.1039/d0tb02507k
DO - 10.1039/d0tb02507k
M3 - 文章
C2 - 33393541
AN - SCOPUS:85100465790
SN - 2050-750X
VL - 9
SP - 983
EP - 991
JO - Journal of Materials Chemistry B
JF - Journal of Materials Chemistry B
IS - 4
ER -