AI Article Synopsis
- The article discusses the interaction between quantum dots and α-chymotrypsin, highlighting how quantum dots reduce the enzyme's intrinsic fluorescence by forming complexes.
- It provides quantitative measurements like quenching rate and binding constants, suggesting that the size of quantum dots affects their interaction with the enzyme.
- Additionally, various spectroscopic techniques reveal changes in the enzyme's structure upon interaction, indicating potential for safe use of quantum dots in biological settings.
Article Abstract
In this article, we have examined the direct spectroscopic and microscopic evidence of efficient quantum dots-α-chymotrypsin (ChT) interaction. The intrinsic fluorescence of digestive enzyme is reduced in the presence of quantum dots through ground-state complex formation. Based on the fluorescence data, quenching rate constant, binding constant, and number of binding sites are calculated under optimized experimental conditions. Interestingly, fluorescence quenching method clearly illustrated the size dependent interaction of MPA-CdTe quantum dots. Conformational change of ChT was traced using synchronous fluorescence measurements, circular dichroism and FTIR spectroscopic methods. Furthermore, the AFM results revealed that the individual enzyme molecule dimensions were changed after interacting with quantum dot. Consequently, this result could be helpful for constructing safe and effective utilisation of QDs in biological applications.
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| http://dx.doi.org/10.1002/bio.2847 | DOI Listing |
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