2022
DOI: 10.1021/acsomega.2c02778
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Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues

Abstract: Cecropin P1 (CP1) isolated from a large roundworm Ascaris suum , which is found in pig intestines, has been extensively studied as a model antimicrobial peptide (AMP). However, despite being a model AMP, its antibacterial mechanism is not well understood, particularly the function of its C-terminus. By using an Escherichia coli overexpression system with calmodulin as a fusion partner, we succeeded in the mass expression of recombinant peptides, avoiding toxicity t… Show more

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Cited by 3 publications
(1 citation statement)
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“…First, the sequence modification approach consists of using known AMP sequences as templates and subsequently modifying of one or more amino acids to identify the most crucial amino acids and their positions for antimicrobial activity or to elucidate the role of certain motifs present in the peptide on its overall mechanism of action [105]. Wiradharma et al designed short AMPs by using repeats of hydrophobic and cationic residues known to confer antimicrobial activity.…”
Section: In Silico Design Of Peptidesmentioning
confidence: 99%
“…First, the sequence modification approach consists of using known AMP sequences as templates and subsequently modifying of one or more amino acids to identify the most crucial amino acids and their positions for antimicrobial activity or to elucidate the role of certain motifs present in the peptide on its overall mechanism of action [105]. Wiradharma et al designed short AMPs by using repeats of hydrophobic and cationic residues known to confer antimicrobial activity.…”
Section: In Silico Design Of Peptidesmentioning
confidence: 99%