期刊
NANOSCALE
卷 4, 期 4, 页码 1283-1286出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2nr11541g
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类别
资金
- MOST [2011CB933600]
- NSFC [21073181, 20975098]
- CAS
- Natural Science Foundation of Jilin Province China [201015103]
- Jilin University [200903095]
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.
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