Journal
PROCESS BIOCHEMISTRY
Volume 134, Issue -, Pages 341-350Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2023.09.003
Keywords
Glucose oxidase; Charged short peptide; Structure; Molecular dynamics simulation; Molecular docking
Ask authors/readers for more resources
This study investigated the effects of charged short peptides on the activity and structure of glucose oxidase (GOx). The results showed that negatively charged peptides increased enzyme activity, while positively charged peptides decreased it. The peptides altered the microenvironment and charge arrangement of GOx, resulting in conformational changes and altered enzymatic activity.
Charged short peptides and glucose oxidase (GOx) were studied in this paper to reveal how these peptides alter the activity and structure of GOx. Results showed that the synthesized negatively charged peptides T-8(-) and positively charged peptides T-9(+) could increase and decrease enzyme activity, respectively. The T-8(-) treated GOx potential increased by 33.6%. Meanwhile, the alpha-helix content decreased by 5.5%, and the root mean square deviation (RMSD) value decreased significantly. The fluorescence and UV-visible spectra revealed varying degrees of changes in peak and peak intensity, respectively. Overall, in the absence of contact reactions between T-9(+) and T-8(-) with GOx, the CPs changed the microenvironment around GOx and the charge arrangement on its surface, causing conformational changes in GOx and altering its enzymatic activity. The effect of CPs on GOx was further investigated using the molecular docking technique. After T-8(-) treatment, the number of hydrogen bonds increased from 3 without short peptide treatment to 8
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available