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전다솜,Binu Jacob,곽철희,김양미 대한화학회 2017 Bulletin of the Korean Chemical Society Vol.38 No.11
Papiliocin is a 37-residue antimicrobial peptide, with Trp2 and Phe5 previously reported as key residues necessary for its antibacterial activity. This study determined the essential length of the N-terminal fragment of papiliocin necessary to retain its biological activity. We designed and synthesized an array of seven peptides from the N-terminal helix (PapN), with longest peptide with 22 residues and the shortest peptide consisting of the first 10 residues. The minimum inhibitory concentration (MIC) values and cytotoxicity measurement revealed that a PapN-12mer containing a three-turn, amphipathic helix was the shortest peptide exhibiting antibacterial activity without cytotoxicity. Additionally, PapN-20mer peptide containing two isoleucines at the C-terminus represented the shortest peptide exhibiting potent anti-inflammatory activities by inhibiting nitric oxide production and inflammatory cytokine production in lipopolysaccharide-stimulated mouse macrophage RAW264.7 cells. These results provided valuable insights into the design of short, potent peptide analogs of papiliocin.
Poly-lysine peptidomimetics having potent antimicrobial activity without hemolytic activity
Ahn, Mija,Jacob, Binu,Gunasekaran, Pethaiah,Murugan, Ravichandran N.,Ryu, Eun Kyoung,Lee, Ga-hyang,Hyun, Jae-Kyung,Cheong, Chaejoon,Kim, Nam-Hyung,Shin, Song Yub,Bang, Jeong Kyu Springer-Verlag 2014 Amino acids Vol.46 No.9