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Identification and elucidation of proline-rich antimicrobial peptides with enhanced potency and delivery.

ABSTRACT: Proline-rich antimicrobial peptides (PrAMPs) kill bacteria via a nonlytic mechanism in which they permeate through the outer membrane, utilize protein-mediated transport across the inner membrane, and target the ribosome to inhibit protein synthesis. We previously reported that substitutions of oncocin ( VDKPPYLPRPRPPRRIYNR-NH2 ) with a pair of cationic residues improved the antimicrobial activity. In this study, we applied the design protocol to three other PrAMPs: apidaecin-1b, pyrrhocoricin, and bactenecin 7(1-16) and found that the substitutions (R4K and I8K/R) for apidaecin-1b improve the activity by twofold (p?

SUBMITTER: Lai PK 

PROVIDER: S-EPMC6726534 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Identification and elucidation of proline-rich antimicrobial peptides with enhanced potency and delivery.

Lai Pin-Kuang PK   Tresnak Daniel T DT   Hackel Benjamin J BJ  

Biotechnology and bioengineering 20190721 10

Proline-rich antimicrobial peptides (PrAMPs) kill bacteria via a nonlytic mechanism in which they permeate through the outer membrane, utilize protein-mediated transport across the inner membrane, and target the ribosome to inhibit protein synthesis. We previously reported that substitutions of oncocin ( VDKPPYLPRPRPPRRIYNR-NH2 ) with a pair of cationic residues improved the antimicrobial activity. In this study, we applied the design protocol to three other PrAMPs: apidaecin-1b, pyrrhocoricin,  ...[more]

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