Jump to main content
Jump to site search

Issue 33, 2017
Previous Article Next Article

Enzymatic activity inside a DNA/peptide complex

Author affiliations


The mutual interaction between enzymes and their environments plays a key role in various life processes. In this study, using the complexes formed by salmon DNA and a de novo designed peptide, Ac-RRRRRRRRRGALGLPGKGGGLQRLTALDGR-NH2 (abbreviated as RR-30), as a model, we studied the activity of collagenase encapsulated inside the complex. Collagenase is able to cleave RR-30 at a LG/LP site, generating two shorter length peptides, which decreases the stability of the complex. Results show that the complex dissociates with time in the presence of collagenase. The dissociation rate is linearly proportional to the collagenase concentration. On the other hand, the collagenase activity is severely deteriorated inside the complex, where only 1/3 of the enzyme is active. We attribute it to the electrostatic interaction and hydrophobic interaction between collagenase and the components of the complex. Therefore, the mutual interaction determines the structure and kinetics of the DNA/peptide complex.

Graphical abstract: Enzymatic activity inside a DNA/peptide complex

Back to tab navigation

Supplementary files

Publication details

The article was received on 16 Jun 2017, accepted on 01 Aug 2017 and first published on 01 Aug 2017

Article type: Paper
DOI: 10.1039/C7CP04066K
Citation: Phys. Chem. Chem. Phys., 2017,19, 22487-22493
  •   Request permissions

    Enzymatic activity inside a DNA/peptide complex

    W. Pan, H. Wen and D. Liang, Phys. Chem. Chem. Phys., 2017, 19, 22487
    DOI: 10.1039/C7CP04066K

Search articles by author