Journal
ACS CHEMICAL BIOLOGY
Volume 10, Issue 4, Pages 965-969Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb501057d
Keywords
-
Categories
Funding
- Ministero dell' Istruzione, dell'Universita e dellaRicerca (MIUR) [PRIN 2010 2010M2JARJ_002, MERIT RBNE08HWLZ_014]
Ask authors/readers for more resources
We here report an original approach to elucidate mechanisms of action of antimicrobial peptides and derive crucial structural requirements for the design of novel therapeutic agents. The high resolution structure of TB_KKG6A, an antimicrobial peptide designed to amplify the spectrum of action of Temporin B, bound to E. coli is here determined by means of CD and NMR methodologies. We have also defined, through STD analysis, the residues in closer proximity to the bacterial membrane
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