Related Experiment Video
Updated: May 11, 2026
11:25
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
Published on: March 18, 2017
Human cathelicidin peptide LL37 binds telomeric G-quadruplex.
Jagannath Jana1, Rajiv Kumar Kar, Anirban Ghosh
1Biomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII M, Kolkata, India.
Molecular Biosystems
|May 3, 2013
Summary
The antimicrobial peptide LL37 binds to G-quadruplex structures, which can inhibit telomerase activity in cancer cells. This finding suggests LL37 as a potential therapeutic agent for cancer treatment.
Area of Science:
- Biochemistry
- Molecular Biology
- Antimicrobial Peptides
Background:
- Telomerase is a key enzyme in cancer cell proliferation.
- G-quadruplex structures are potential targets for cancer therapy.
- Host defense peptides have diverse biological activities.
Purpose of the Study:
- To investigate the interaction between LL37 and G-quadruplex structures.
- To determine if LL37 binding to G-quadruplexes affects telomerase activity.
Main Methods:
- G-quadruplex binding assays.
- Telomerase activity assays.
Main Results:
- LL37 was identified as a potent binder of G-quadruplex structures.
- Stabilization of G-quadruplex by LL37 inhibits telomerase activity.
Conclusions:
- LL37 shows potential as a G-quadruplex stabilizer.
- LL37 represents a promising therapeutic candidate for targeting telomerase in cancer.
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