Regular Article |
|
|
|
|
|
Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1 |
Li DONGa,c, Juan-Juan YANGb, Ying WANGa,c, Huan LIUa, Li-Xian MUa,c, Dong-Hai LINb, Ren LAIa |
a Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China; b Department of Chemistry, College of Chemistry and Chemical Engineering, and the Key Laboratory for Chemical Biology of Fujian Province, Xiamen University, Xiamen 361005, Fujian, China; c Graduate University of Chinese Academy of Sciences, Beijing 100049, China |
|
|
Abstract Cathelicidin Pc-CATH1 is a cathelicidin-derived myeloid antimicrobial peptide identified from Phasianus colchicus with strong antimicrobial activity against most of bacteria and fungi tested, including the clinically isolated(IS) drug-resistant strains. Considering the uniform distribution of net positive charge in both C-and N-terminus sequence of cathelicidin Pc-CATH1 and most of hydrophobic amino acid(aa) residues positioned in middle of the sequence, the antimicrobial peptide was used to investigate the structure-function relationship by truncating gradually N-or C-terminus amino acid residue. More than 10 modified peptide homologues(20-26 aa length) of cathelicidin Pc-CATH1 were found to keep strong antimicrobial abilities. The possible relationships between bioactivities including antimicrobial and hemolytic abilities, components of secondary structure, hydrophobicity, amphipathicity, net charge, and sequence length were investigated. The current work provided suggestions for structural and functional modification of linear, α-helical antimicrobial peptides containing no disulfided bridges.
|
Keywords
cathelicidin
antimicrobial peptide
structure-function relationship
|
Fund:This work was supported by Chinese National Natural Science Foundation(31070701, 31000962, 31025025, 30730026), the Program of Shanghai Subject Chief Scientist(NO. 09XD1405100), the Ministry of Science and Technology(2010CB529800, 2009ZX09103-1/091, 2011ZX09102-002-10) and the Ministry of Agriculture(2009ZX08009-159B). |
Issue Date: 11 February 2018
|
|
|
[1] |
Shi, Q. W.; Su, X. H.; Kiyota, H. Chem. Rev. 2008, 108, 4295-4327.
|
|
Zasloff, M. Nature 2002, 415, 389-395.
|
[2] |
Bulet, P.; Stocklin, R.; Menin, L. Immunol. Rev. 2004, 198, 169-184.
|
[3] |
Yamasaki, K.; Gallo, R. L. Eur. J. Dermatol. 2008, 18, 11-21.
|
[4] |
Ritonja, A.; Kopitar, M.; Jerala, R.; Turk, V. FEBS. Lett. 1989, 255, 211-214.
|
[5] |
Tomasinsig, L.; Zanetti, M. Curr. Protein. Pept. Sci. 2005, 6, 23-34.
|
[6] |
Wang, Y.; Lu, Z.; Feng, F.; Zhu, W.; Guang, H.; Liu, J.; He, W.; Chi, L.; Li, Z.; Yu, H. Dev. Comp. Immunol. 2011, 35, 314-322.
|
[7] |
Ghosh, A. K.; Rukmini, R.; Chattopadhyay, A. Biochemistry 1997, 36, 14291-14305.
|
[8] |
Yu, K.; Kang, S.; Park, N.; Shin, J.; Kim, Y. J. Pept. Res. 2000, 55, 51-62.
|
[9] |
Lim, S. S.; Kim, Y.; Park, Y.; Kim, J. L.; Park, I. S.; Hahm, K. S.; Shin, S.Y. Biochem. Biophys. Res. Commun. 2005, 334, 1329-1335.
|
[10] |
Kim, J. K.; Lee, E.; Shin, S.; Jeong, K. W.; Lee, J. Y.; Bae, S. Y.; Kim, S. H.; Lee, J.; Kim, S. R.; Lee, D. G.; Hwang, J. S.; Kim, Y. J. Biol. Chem. 2011, 286, 41296-41311.
|
[11] |
Gautier, R.; Douguet, D.; Antonny, B.; Drin, G. Bioinformatics 2008, 24, 2101-2102.
|
[12] |
Bignami, G. S. Toxicon 1993, 31, 817-820.
|
[13] |
Chang, C. T.; Wu, C. S.; Yang, J. T. Anal. Biochem. 1978, 91, 13-31
|
[14] |
Lai, R.; Zheng, Y. T.; Shen, J. H.; Liu, G. J.; Liu, H.; Lee, W. H.; Tang, S. Z.; Zhang, Y. Peptides 2002, 23, 427-435.
|
[15] |
Li, J. X.; Zhang, C.; Xu, X. Q.; Wang, J.; Yu, H. N.; Lai, R.; Gong, W. M. Faseb J. 2007, 21, 2466-2473.
|
[16] |
Li, J. X.; Xu, X. Q.; Xu, C. H.; Zhou, W. P.; Zhang, K. Y.; Yu, H. N.; Zhang,Y. P.; Zheng, Y. T.; Rees, H. H.; Lai, R.; Yang, D. M.; Wu, J. Mol. Cell. Proteomics 2007, 6, 882-894.
|
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
|
Shared |
|
|
|
|
|
Discussed |
|
|
|
|