Journal
PEPTIDES
Volume 68, Issue -, Pages 197-204Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2014.09.011
Keywords
Hyphantria cunea; Antibacterial peptide; ABP-dHC-cecropin A; Molecular structure; Antibacterial activity
Funding
- National 863 Program of China [2013AA102703]
- International Science 82 Technology Cooperation Program of China [2014DFG32440]
- Graduate Innovative Project of Jiangsu Province [CXZZ13_0530]
- Doctoral Degree Thesis Innovation Foundation of Nanjing Forestry University [2013Y07]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- Program for Innovative Research Team in University of Educational Department and Jiangsu Province, China
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The increasing resistance of bacteria and fungi to currently available antibiotics is a major concern worldwide, leading to enormous efforts to develop new antibiotics with new modes of actions. In this paper, cDNA encoding cecropin A was amplified from drury (Hyphantria cunea) (dHC) pupa fatbody total RNA using RT-PCR. The full-length dHC-cecropin A cDNA encoded a protein of 63 amino acids with a predicted 26-amino acid signal peptide and a 37-amino acid functional domain. We synthesized the antibacterial peptide (ABP) from the 37-amino acid functional domain (ABP-dHC-cecropin A), and amidated it via the C-terminus. Time-of-flight mass spectrometry showed its molecular weight to be 4058.94. The ABP-dHC-cecropin A was assessed in terms of its protein structure using bioinformatics and CD spectroscopy. The protein's secondary structure was predicted to be a-helical. In an antibacterial activity analysis, the ABP-dHC-cecropin A exhibited strong antibacterial activity against E. coli K12D31 and Agrobacterium EHA105. (C) 2014 Elsevier Inc. All rights reserved.
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