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Updated: Apr 23, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Purification and characterization of a novel antimicrobial peptide from sheep reproductive tract
Chen Chen1, Chaofeng Ku, Xinwen Bo
1College of Biological Science and Engineering, Shaanxi University of Technology, Hanzhong, 723000, Shaanxi, China, cchen2008@yahoo.com.
Abstract:
A novel antimicrobial peptide, SRTAP-40 has been purified and characterized from sheep reproductive tract. The isolation procedure entailed acetic acid extraction, gel filtration chromatography, and HPLC. SRTAP-40 is composed of 40 amino acid residues with a MW of 4,820.47 Da from MALDI-TOF-MS. Its N-terminal sequence was AYVLDEPKP. SRTAP-40 cDNA was cloned by 3'-RACE. SRTAP-40 showed activity against E. coli Staphylococcus aureus, Streptococcus sp. and, Candida albicans with MIC values of 12, 12, 24, 6 μg/ml, respectively. By BLAST search, SRTAP-40 had no significant similarity to any known peptide.
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