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Tuning the Activity of Anoplin by Dendrimerization of Lysine and Lipidation of the N-Terminal.

ABSTRACT: Dendrimeric antimicrobial peptides or lipopeptides have strong transmembrane ability and antibacterial activity. To obtain some ideal antimicrobial peptides, anoplin, a natural antimicrobial peptide with weak antimicrobial activity, was modified by C-terminal dendrimerization using lysine and N-terminal lipidation using fatty acids. 2K-3A-C4, a trimer of anoplin, was dendrimerized by two lysines at the C-terminal and was lipidated by n-butyric acid at the N-terminal, and thus exhibited the best antibacterial activity. However, the trimer had high hemolytic activity. Finally, A-C8, a simple structural lipopeptide, which is not a dendrimer, was obtained following the lipidation of anoplin using octanoic acid; it exhibited the highest therapeutic index, which makes it a probable antibiotic and thus was screened out.

SUBMITTER: Gou S

PROVIDER: S-EPMC8387982 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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Tuning the Activity of Anoplin by Dendrimerization of Lysine and Lipidation of the N-Terminal.

Gou Sanhu S Li Beibei B Ouyang Xu X Ba Zufang Z Zhong Chao C Ni Jingman J

ACS omega 20210812 33

Dendrimeric antimicrobial peptides or lipopeptides have strong transmembrane ability and antibacterial activity. To obtain some ideal antimicrobial peptides, anoplin, a natural antimicrobial peptide with weak antimicrobial activity, was modified by C-terminal dendrimerization using lysine and N-terminal lipidation using fatty acids. 2K-3A-C4, a trimer of anoplin, was dendrimerized by two lysines at the C-terminal and was lipidated by <i>n</i>-butyric acid at the N-terminal, and thus exhibited th ...[more]

PMID: 34471740

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