Abstract
The effect of N-acetyl-l-cysteine-capped CdTe quantum dots (NAC-CdTe QDs) with different sizes on lysozyme was investigated by isothermal titration calorimetry (ITC), enzyme activity assays, and multi-spectroscopic methods. ITC results proved that NAC-CdTe QDs can spontaneously bind with lysozyme and hydrophobic force plays a major role in stabilizing QDs-lysozyme complex. Multi-spectroscopic measurements revealed that NAC-CdTe QDs caused strong quenching of the lysozyme's fluorescence in a size-dependent quenching manner. Moreover, the changes of secondary structure and microenvironment in lysozyme caused by the NAC-CdTe QDs were higher with a bigger size. The results of enzyme activity assays showed that the interaction between lysozyme and NAC-CdTe QDs inhibited the activity of lysozyme and the inhibiting effect was in a size-dependent manner. Based on these results, we conclude that NAC-CdTe QDs with larger particle size had a larger impact on the structure and function of lysozyme.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
