Abstract:
OBJECTIVES:To identify and characterize a novel antimicrobial peptide, catesbeianin-1. RESULTS:Catesbeianin-1 is 25 amino acids long and is α-helical, cationic and amphipathic. It had antimicrobial activity against Gram-positive and Gram-negative bacteria. It was resistant against trypsin and pepsin. Catesbeianin-1 exhibited moderate hemolytic activity (approx 8%) at 100 μg/ml, and its HC50 (50% hemolytic concentration) was 300 μg/ml. Its cytotoxicity was approx 10-20% at 100 μg/ml, and its CC50 (50% cytotoxic concentration) was >100 μg/ml. The LD50 of catesbeianin-1 in mice was 80 mg/kg. At 3.1 µg/ml, catesbeianin-1 significantly inhibited the growth of methicillin-resistant Staphylococcus aureus. CONCLUSIONS:A new antimicrobial peptide from the skin of Lithobates catesbeianus (American bullfrog) may represent a template for the development of novel antimicrobial agents.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Xu H,Zhang Y,Feng X,Tie K,Cao Y,Han Wdoi
10.1007/s10529-017-2312-7subject
Has Abstractpub_date
2017-06-01 00:00:00pages
897-903issue
6eissn
0141-5492issn
1573-6776pii
10.1007/s10529-017-2312-7journal_volume
39pub_type
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journal_title:Biotechnology letters
pub_type: 杂志文章
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journal_title:Biotechnology letters
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2012-06-01 00:00:00
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pub_type: 杂志文章
doi:10.1023/b:bile.0000030050.20353.a6
更新日期:2004-06-01 00:00:00
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pub_type: 杂志文章
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更新日期:2005-04-01 00:00:00
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更新日期:2003-03-01 00:00:00
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journal_title:Biotechnology letters
pub_type: 杂志文章
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更新日期:2018-01-01 00:00:00
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pub_type: 杂志文章,评审
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更新日期:2010-11-01 00:00:00
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journal_title:Biotechnology letters
pub_type: 杂志文章
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更新日期:2006-12-01 00:00:00