Journal
NANOSCALE
Volume 4, Issue 4, Pages 1283-1286Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2nr11541g
Keywords
-
Categories
Funding
- MOST [2011CB933600]
- NSFC [21073181, 20975098]
- CAS
- Natural Science Foundation of Jilin Province China [201015103]
- Jilin University [200903095]
Ask authors/readers for more resources
To determine the effects of biophysical parameters (e.g. charge, hydrophobicity, helicity) of peptides on the mechanism of anticancer activity, we applied a single molecule technique-force spectroscopy based on atomic force microscope (AFM)-to study the interaction force at the single molecule level. The activity of the peptide and analogs against HeLa cells exhibited a strong correlation with the hydrophobicity of peptides. Our results indicated that the action mode between alpha-helical peptides and cancer cells was largely hydrophobicity-dependent.
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