期刊
ACS CHEMICAL BIOLOGY
卷 10, 期 4, 页码 965-969出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb501057d
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资金
- Ministero dell' Istruzione, dell'Universita e dellaRicerca (MIUR) [PRIN 2010 2010M2JARJ_002, MERIT RBNE08HWLZ_014]
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
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