Repository logo
Log in(current)
Repository logoMIT Open ScholarshipDSpace@MIT
  1. Home
  2. MIT Open Access Articles
  3. MIT Open Access Articles
  4. Effects of Lipidation on a Proline-Rich Antibacterial Peptide

Effects of Lipidation on a Proline-Rich Antibacterial Peptide

Thumbnail Image
Download
Name

ijms-22-07959.pdf

Size

2.09 MB

Format

Unknown

Checksum (MD5)

970508cb41fd4770a7ef11fece7d9a73

Download all files submitted through automated deposit
packager-610d52f5.zip (962.23 KB)
Author(s)
Armas, Federica
Date Issued
July 26, 2021
Journal
International journal of molecular sciences
Publisher
Multidisciplinary Digital Publishing Institute
Citation
International Journal of Molecular Sciences 22 (15): 7959 (2021)
Version
Final published version
Abstract
The emergence of multidrug-resistant bacteria is a worldwide health problem. Antimicrobial peptides have been recognized as potential alternatives to conventional antibiotics, but still require optimization. The proline-rich antimicrobial peptide Bac7(1-16) is active against only a limited number of Gram-negative bacteria. It kills bacteria by inhibiting protein synthesis after its internalization, which is mainly supported by the bacterial transporter SbmA. In this study, we tested two different lipidated forms of Bac7(1-16) with the aim of extending its activity against those bacterial species that lack SbmA. We linked a C12-alkyl chain or an ultrashort cationic lipopeptide Lp-I to the C-terminus of Bac7(1-16). Both the lipidated Bac-C12 and Bac-Lp-I forms acquired activity at low micromolar MIC values against several Gram-positive and Gram-negative bacteria. Moreover, unlike Bac7(1-16), Bac-C12, and Bac-Lp-I did not select resistant mutants in E. coli after 14 times of exposure to sub-MIC concentrations of the respective peptide. We demonstrated that the extended spectrum of activity and absence of de novo resistance are likely related to the acquired capability of the peptides to permeabilize cell membranes. These results indicate that C-terminal lipidation of a short proline-rich peptide profoundly alters its function and mode of action and provides useful insights into the design of novel broad-spectrum antibacterial agents.
MIT Department
Singapore-MIT Alliance in Research and Technology (SMART)
Terms of Use
Creative Commons Attribution
https://creativecommons.org/licenses/by/4.0/
Persistent DSpace Link
https://hdl.handle.net/1721.1/133210.2
DOI of Published Version
https://doi.org/10.3390/ijms22157959
Repository logo
PrivacyPermissionsAccessibilityContact us
Repository logo
Notify us about copyright concerns.