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Carbon Dots/Cu 2 O Composite with Intrinsic High Protease‐Like Activity for Hydrolysis of Proteins under Physiological Conditions
Author(s) -
Li Bin,
Chen Daomei,
Nie Minfang,
Wang Jiaqiang,
Li Yizhou,
Yang Yepeng
Publication year - 2018
Publication title -
particle and particle systems characterization
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 56
eISSN - 1521-4117
pISSN - 0934-0866
DOI - 10.1002/ppsc.201800277
Subject(s) - protease , hydrolysis , bovine serum albumin , trypsin , proteases , chemistry , nanomaterials , casein , peptide , peptide bond , enzyme , combinatorial chemistry , biochemistry , nanotechnology , materials science
Whereas a variety of inorganic nanomaterials possessing intrinsic peroxidase‐like activity have recently attracted considerable interest, little attention is given to explore their intrinsic protease‐mimic activities. And the construction of efficient enzyme mimetics for the hydrolysis of peptide bonds in proteins still represents a major technical challenge due to the high stability of peptide bonds and the importance of proteases in biology and industry. Herein, it is described for the first time that Cu 2 O‐decorated carbon quantum dots (CQDs/Cu 2 O) possess an intrinsic protease‐mimic activity to hydrolyze proteins including bovine serum albumin (BSA) and casein under physiological conditions. CQDs/Cu 2 O also features a desirable stability and good reusability. CQDs/Cu 2 O has a much higher affinity for BSA than trypsin. To the best of knowledge, this is the first example of protein hydrolysis by stable composite nanomaterials under physiological conditions which may open this catalytic system for a multitude of potential applications in biological systems.