Functional Analysis of Hybrid Peptide CAMA-Syn: Expression in Mammalian Cells and Antimicrobial Potential
Authors: Zhang, Junlin; Peng, Sha; Cheng, Xiang; Wang, Huayan
Source: Protein and Peptide Letters, Volume 19, Number 10, October 2012 , pp. 1076-1081(6)
Publisher: Bentham Science Publishers
Abstract:CAMA-syn, a hybrid composed of N-terminal α-helical segment of Cecropin A(amino acid 1-8) and Magainin 2 (amino acid 1-12), is a novel small peptide with the potent antibacterial and synergistic activity without cytotoxicity. In order to test the antibacterial function of CAMA-syn produced in mammalian cells, several vectors containing the synthesized CAMA-syn DNA fragment were constructed and transfected into recipient cells. The results showed that CAMAsyn fusion to green fluorescent protein (GFP) or to hemagglutinin epitope (HA) tag was expressed in both bovine embryo fibroblasts (BEF) and mouse macrophage RAW264.7 cells. The antibacterial assays of CAMA-syn were conducted against both Gram positive and negative bacteria, including S. abortusovis, P. anatis, S. hyicus and S. suis. The results of colony-forming efficiency and cell growth curves proved that the in vitro expressed CAMA-syn could have the antibacterial activity, demonstrating that macrophage specific expression of antimicrobial peptide CAMA-syn could inhibit the growth of bacteria.
Document Type: Research Article
Publication date: October 1, 2012
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.