Purification and cDNA Cloning of Antimicrobial Peptides from the Skin Secretion of the Chinese Frog Rana chensinensis
Autor: | Yang He, Wang Yuhua, Bo Lv, Liankui Wen, Huan Wang, Djerry Yvan Arold Dinghani, Manyu Wu, Hu Yaohui, Yu Hansong, Bixiang Wang |
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Rok vydání: | 2020 |
Předmět: |
chemistry.chemical_classification
biology Edman degradation 010405 organic chemistry Rana chensinensis Antimicrobial peptides Bioengineering Peptide biology.organism_classification Antimicrobial 01 natural sciences Biochemistry 0104 chemical sciences Analytical Chemistry Amino acid chemistry Complementary DNA Drug Discovery Molecular Medicine Antibacterial activity |
Zdroj: | International Journal of Peptide Research and Therapeutics. 27:293-300 |
ISSN: | 1573-3904 1573-3149 |
DOI: | 10.1007/s10989-020-10074-y |
Popis: | The skin secretions of amphibians are a rich source of bioactive peptides. We isolated chensirin-1 and chensirin-2 from the skin secretion of the Chinese frog Rana chensinensis. Sephadex-G-50 and RP-HPLC were employed to purify these peptides. The amino acid sequences of these peptides were VLPLVGNLLNDLLGE and IIPLPLGYFAKKT, respectively, as determined by Edman degradation. The molecular weights were 1578.7 and 1460.8 Da, respectively, as analyzed by HPLC-ESI-MS. The chensirin cDNA was cloned by 5′ and 3′ amplification of cDNA ends, synthesized and purified. The antibacterial activities of the chensirins were tested using minimum inhibitory concentration, the results indicated that chensirins inhibit the growth of gram-negative and gram-positive bacteria. Among them, chensirin-1 is a novel peptide with a higher antibacterial activity compared to other similar antimicrobial peptides. These low molecular weight peptides with good antimicrobial efficacy are considered potential sources for developing new antimicrobial agents to improve traditional drug resistance. |
Databáze: | OpenAIRE |
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