Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 58, Issue 21, Pages 8553-8563Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jmedchem.5b01142
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- Brazilian National Council for Scientific and Technological Development (CNPq)
- Ministry of Science and Technology
- Coordination for the Improvement of Higher Education Personnel (CAPES)
- Spanish Ministry of Economy and Competitiveness (MINECO) [SAP 201124899]
- Generalitat de Catalunya [SGR2009-00492]
- MINECO [CTQ2011-22514, FPI BES-2012-057717]
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In silico dissection of crotalicidin (Ctn), a cathelicidin from a South American pit viper, yielded fragments Ctn[1-14] and Ctn[15-34], which were tested to ascertain to what extent they reproduced the structure and activity of the parent peptide. NMR data showing Ctn to be alpha-helical at the N-terminus and unstructured at the C-terminus were matched by similar data from the fragments. The peptides were tested against Gram-positive and -negative bacteria and for toxicity against both tumor and healthy cells. Despite its amphipathic alpha-helical structure, Ctn[1-14] was totally inert toward bacteria or eukaryotic cells. In contrast, unstructured Ctn[15-34] replicated the activity of parent Ctn against Gram-negative bacteria and tumor cells while being significantly less toxic toward eukaryotic cells. This selectivity for bacteria and tumor cells, plus a stability to serum well above that of Ctn, portrays Ctn[15-34] as an appealing candidate for further development as an anti-infective or antitumor lead.
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