Insights into the effect of N-acetyl-L-cysteine-capped CdTe quantum dots on the structure and activity of human serum albumin by spectroscopic techniques

摘要: Abstract Quantum dots (QDs) are a kind of nanostructured semiconductor crystals with the size range 1–10 nm. Their unique photophysical properties and potential toxicity to human health have aroused wide concern scientists general public. However, interaction mechanism QDs on serum albumin (HSA, vital protein in blood) from both structural functional perspectives is rarely reported. In present work, effects N-acetyl- L -cysteine-capped CdTe quantum fluorescence emission peak at 612 nm (QDs-612) conformation function HSA were investigated by spectroscopic methods, molecular docking study esterase activity assay. The hydrophobic between QDs-612 was spontaneous binding constants calculated be 6.85×105 L mol−1 (298 K) 8.89×105 L mol−1 (308 K). induced static quenching changes secondary structure microenvironment Tyr-411 residue, which resulted serious decrease hydrolysis substrate p-nitrophenylacetate assay HSA. This work confirms possibility direct obtains possible relationship