Báo cáo khoa học: Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4
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Gaegurin 4 (GGN4), a 37-residue antimicrobial peptide,consists of two amphipathic ahelices (residues 2–10and16–32) connected by a flexible loop region (residues 11–15). As part of an effort to develop new peptide antibioticswith low molecular mass, the activities of C-terminallytruncated GGN4 analogues were tested. D24)37GGN4, apeptide analogue with 14 residues truncated from theC-terminus of GGN4, showed a complete loss of anti-microbial activity.
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Báo cáo khoa học: Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4
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