Study on biological characteristics and stability of the linear derivative Bac2a from bactenecin_Journal of Biomedical Engineering

Authors：

LI Yingying ¹ , HAN Wanjun ¹ , CAO Songsong ¹ ,  HOU Juncai ¹ , JIANG Zhanmei ¹ , JIANG Chenggang ² , WANG Haimei ¹ , PANG Shiyue ¹

1. College of Food Science, Northeast Agricultural University, Harbin 150030, P.R.China;
2. Harbin Veterinary Research Institute, CAAS, Harbin 150001, P.R.China;

Corresponding author：

HOU Juncai, Email: jchou@neau.edu.cn

Keywords：

Bac2a peptides; antibacterial activity; hemolytic activity; cytotoxicity; stability

DOI：

10.7507/1001-5515.201609002

Video：

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Abstract Full text Figures/Tables Video References Cited by

The objective of the study is to analyze the biological characteristics and stability of the linear derivative Bac2a from bactenecin, compared with the control peptide melittin. The secondary structure, antibacterial activity, hemolytic activity, cell toxicity and stability of the Bac2a were determined by circular dichroism spectroscopy, broth micro-dilution method and MTT assay. The results showed that Bac2a was a nonregular curl in aqueous solution, however, it was an α-helix structure in the hydrophobic environment. The minimal inhibitory concentration (MIC) of Bac2a ranged from 2 to 32 μmol/L, so the bacteriostatic activity of Bac2a was strong. The hemolytic rate was only 14.81% when the concentration of Bac2a was 64 μmol/L, which showed that the hemolytic rate of Bac2a was low. The therapy index of Bac2a was 3.26, and the cytotoxicity was relatively low, thus the cell selectivity was relatively high. In addition, with the heating treatment of 100℃ for 1 h, Bac2a still possessed rather a high antibacterial activity and showed a good heating stability. In a word, Bac2a has good application prospects in food, medicine and other fields, and is expected as a substitute for traditional antibiotics.

Citation： LI Yingying, HAN Wanjun, CAO Songsong, HOU Juncai, JIANG Zhanmei, JIANG Chenggang, WANG Haimei, PANG Shiyue. Study on biological characteristics and stability of the linear derivative Bac2a from bactenecin. Journal of Biomedical Engineering, 2017, 34(4): 572-577. doi: 10.7507/1001-5515.201609002 Copy

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2.	韩文瑜, 孙长江. 抗菌肽的研究现状与展望. 中国兽药杂志, 2009, 43(10): 11-19.
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4.	Cho J, Choi H, Lee D G. Influence of the N- and C-terminal regions of antimicrobial peptide pleurocidin on antibacterial activity. J Microbiol Biotechnol, 2012, 22(10): 1367-1374.
5.	Wu M, Hancock R E. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. Antimicrob Agents Chemother, 1999, 43(5): 1274-1276.
6.	张冰清, 刘晓波. 蜂毒的主要成分及药理作用的研究进展. 药学研究, 2016, 35(3): 172-174.
7.	Wiradharma N, Liu S Q, Yang Y Y. Branched and 4-arm starlike α-helical peptide structures with enhanced antimicrobial potency and selectivity. Small, 2012, 8(3): 362-366.
8.	Hoffknecht B C, Prochnow P, Bandow J E, et al. Influence of metallocene substitution on the antibacterial activity of multivalent peptide conjugates. J Inorg Biochem, 2016, 160: 246-249.
9.	Li Weizhong, Tan Tingting, Xu Wei, et al. Rational design of mirror-like peptides with alanine regulation. Amino Acids, 2016, 48(2): 403-417.
10.	白希希. 新型抗菌肽的设计与研究——生物活性及与磷脂膜相互作用. 郑州: 郑州大学, 2013.
11.	枚春成(Mai Xuan Thanh). 二级结构对抗菌肽的抗菌活性及特异性的影响. 长春: 吉林大学, 2013.
12.	Smith V J, Desbois A P, Dyrynda E A. Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae. Mar Drugs, 2010, 8(4): 1213-1262.
13.	Pandey B K, Ahmad A, Asthana N, et al. Cell-selective lysis by novel analogues of melittin against human red blood cells and Escherichia coli. Biochemistry, 2010, 49(36): 7920-7929.
14.	Yount N Y, Andrés M T, Fierro J F, et al. The γ-core motif correlates with antimicrobial activity in cysteine-containing kaliocin-1 originating from transferrins. Biochim Biophys Acta, 2007, 1768(11): 2862-2872.
15.	Song Y S, Kang J H, Jang S Y, et al. Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim Biophys Acta, 2000, 1463(2): 209-218.
16.	Chou S, Shao Changxuan, Wang Jiajun, et al. Short, multiple-stranded β-hairpin peptides have antimicrobial potency with high selectivity and salt resistance. Acta Biomater, 2016, 30: 78-93.
17.	Zhu Xin, Zhang Licong, Wang Jue, et al. Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity. Acta Biomater, 2015, 18(4): 155-167.
18.	Ma Qingquan, Dong Na, Shan Anshan, et al. Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units. Amino Acids, 2012, 43(6): 2527-2536.

1. O’Connor P M, Ross R P, Hill C, et al. Antimicrobial antagonists against food pathogens: a bacteriocin perspective. Current Opinion in Food Science, 2015, 2(4): 51-57.
2. 韩文瑜, 孙长江. 抗菌肽的研究现状与展望. 中国兽药杂志, 2009, 43(10): 11-19.
3. 丁永林. Bac8c 对口腔主要致龋菌抗菌敏感性研究. 西安: 第四军医大学, 2013.
4. Cho J, Choi H, Lee D G. Influence of the N- and C-terminal regions of antimicrobial peptide pleurocidin on antibacterial activity. J Microbiol Biotechnol, 2012, 22(10): 1367-1374.
5. Wu M, Hancock R E. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. Antimicrob Agents Chemother, 1999, 43(5): 1274-1276.
6. 张冰清, 刘晓波. 蜂毒的主要成分及药理作用的研究进展. 药学研究, 2016, 35(3): 172-174.
7. Wiradharma N, Liu S Q, Yang Y Y. Branched and 4-arm starlike α-helical peptide structures with enhanced antimicrobial potency and selectivity. Small, 2012, 8(3): 362-366.
8. Hoffknecht B C, Prochnow P, Bandow J E, et al. Influence of metallocene substitution on the antibacterial activity of multivalent peptide conjugates. J Inorg Biochem, 2016, 160: 246-249.
9. Li Weizhong, Tan Tingting, Xu Wei, et al. Rational design of mirror-like peptides with alanine regulation. Amino Acids, 2016, 48(2): 403-417.
10. 白希希. 新型抗菌肽的设计与研究——生物活性及与磷脂膜相互作用. 郑州: 郑州大学, 2013.
11. 枚春成(Mai Xuan Thanh). 二级结构对抗菌肽的抗菌活性及特异性的影响. 长春: 吉林大学, 2013.
12. Smith V J, Desbois A P, Dyrynda E A. Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae. Mar Drugs, 2010, 8(4): 1213-1262.
13. Pandey B K, Ahmad A, Asthana N, et al. Cell-selective lysis by novel analogues of melittin against human red blood cells and Escherichia coli. Biochemistry, 2010, 49(36): 7920-7929.
14. Yount N Y, Andrés M T, Fierro J F, et al. The γ-core motif correlates with antimicrobial activity in cysteine-containing kaliocin-1 originating from transferrins. Biochim Biophys Acta, 2007, 1768(11): 2862-2872.
15. Song Y S, Kang J H, Jang S Y, et al. Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim Biophys Acta, 2000, 1463(2): 209-218.
16. Chou S, Shao Changxuan, Wang Jiajun, et al. Short, multiple-stranded β-hairpin peptides have antimicrobial potency with high selectivity and salt resistance. Acta Biomater, 2016, 30: 78-93.
17. Zhu Xin, Zhang Licong, Wang Jue, et al. Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity. Acta Biomater, 2015, 18(4): 155-167.
18. Ma Qingquan, Dong Na, Shan Anshan, et al. Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units. Amino Acids, 2012, 43(6): 2527-2536.

Journal of Biomedical Engineering

Study on biological characteristics and stability of the linear derivative Bac2a from bactenecin

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