Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 19, Issue 1, Pages -Publisher
MDPI
DOI: 10.3390/ijms19010067
Keywords
atomic force microscopy; membrane-active peptide; helicity; hydrophobicity
Funding
- National Natural Science Foundation of China [81373445, 21373200, 21525314]
- Natural Science Foundation of Jilin Province of China [20150101189JC]
- National Key R&D Program of China [2017YFA0505300]
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V13K, a 26-residue peptide, has been shown to have strong antimicrobial activity, negligible hemolytic activity, and significant anticancer activity. In the present work, V13K was used as the framework to investigate the influence of helicity, as influenced by d-amino acid substitutions in the center of the peptide polar and non-polar faces of the amphipathic helix, on biological activity. The antibacterial and anticancer activities of the peptides were investigated. Atomic force microscopy and other biophysical methods were used to investigate the effect of peptide helicity on biological activity. The results showed the importance of suitable and rational modification of membrane-active peptides, based on helicity, in optimizing potential biological activity.
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