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New antimicrobial cystatin C-based peptide active against gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus and multiresistant coagulase-negative staphylococci

Jasir, Aftab LU ; Kasprzykowski, Franciszek ; Kasprzykowska, Regina ; Lindström, Veronica LU orcid ; Schalén, Claes LU orcid and Grubb, Anders LU orcid (2003) In APMIS : acta pathologica, microbiologica, et immunologica Scandinavica 111(11). p.1004-1010
Abstract

We describe the synthesis and antibacterial properties of a novel antimicrobial peptidyl derivative, (2S)-2-(Nalpha-benzyloxycarbonyl-arginyl-leucylamido-1-[(E)-cinnamoylamido]-3-methylbutane, structurally based upon the inhibitory centre of the human cysteine protease inhibitor, cystatin C. The derivative, here called Cystapep 1, displayed antibacterial activity against several clinically important gram-positive bacteria. It displayed minimal inhibitory and bactericidal concentrations of about 16 microg/ml for both Staphylococcus aureus and Streptococcus pyogenes. In radial agar diffusion assays, groups A, B, C and G streptococci as well as staphylococci were generally susceptible to the action of Cystapep 1, whereas pneumococci and... (More)

We describe the synthesis and antibacterial properties of a novel antimicrobial peptidyl derivative, (2S)-2-(Nalpha-benzyloxycarbonyl-arginyl-leucylamido-1-[(E)-cinnamoylamido]-3-methylbutane, structurally based upon the inhibitory centre of the human cysteine protease inhibitor, cystatin C. The derivative, here called Cystapep 1, displayed antibacterial activity against several clinically important gram-positive bacteria. It displayed minimal inhibitory and bactericidal concentrations of about 16 microg/ml for both Staphylococcus aureus and Streptococcus pyogenes. In radial agar diffusion assays, groups A, B, C and G streptococci as well as staphylococci were generally susceptible to the action of Cystapep 1, whereas pneumococci and enterococci were less susceptible. No activity against gram-negative bacteria was observed. Cystapep 1 also showed high activity against methicillin-resistant S. aureus (MRSA) and multiantibiotic-resistant coagulase-negative staphylococci (CNS), suggesting that its mechanism of action differs from those of most currently used antibiotics.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Anti-Bacterial Agents, Cystatin C, Cystatins, Dipeptides, Drug Resistance, Multiple, Bacterial, Gram-Positive Cocci, Humans, Methicillin Resistance, Microbial Sensitivity Tests, Oligopeptides, Staphylococcus aureus, Streptococcus pyogenes, Journal Article, Research Support, Non-U.S. Gov't
in
APMIS : acta pathologica, microbiologica, et immunologica Scandinavica
volume
111
issue
11
pages
7 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:14629266
  • wos:000187201300002
  • scopus:0346244038
  • pmid:14629266
ISSN
1600-0463
DOI
10.1111/j.1600-0463.2003.t01-1-apm1111110.x
language
English
LU publication?
no
id
e558f3df-406e-4d58-8772-681fe8dfc066 (old id 118762)
date added to LUP
2016-04-01 12:37:56
date last changed
2023-01-03 19:20:15
@article{e558f3df-406e-4d58-8772-681fe8dfc066,
  abstract     = {{<p>We describe the synthesis and antibacterial properties of a novel antimicrobial peptidyl derivative, (2S)-2-(Nalpha-benzyloxycarbonyl-arginyl-leucylamido-1-[(E)-cinnamoylamido]-3-methylbutane, structurally based upon the inhibitory centre of the human cysteine protease inhibitor, cystatin C. The derivative, here called Cystapep 1, displayed antibacterial activity against several clinically important gram-positive bacteria. It displayed minimal inhibitory and bactericidal concentrations of about 16 microg/ml for both Staphylococcus aureus and Streptococcus pyogenes. In radial agar diffusion assays, groups A, B, C and G streptococci as well as staphylococci were generally susceptible to the action of Cystapep 1, whereas pneumococci and enterococci were less susceptible. No activity against gram-negative bacteria was observed. Cystapep 1 also showed high activity against methicillin-resistant S. aureus (MRSA) and multiantibiotic-resistant coagulase-negative staphylococci (CNS), suggesting that its mechanism of action differs from those of most currently used antibiotics.</p>}},
  author       = {{Jasir, Aftab and Kasprzykowski, Franciszek and Kasprzykowska, Regina and Lindström, Veronica and Schalén, Claes and Grubb, Anders}},
  issn         = {{1600-0463}},
  keywords     = {{Anti-Bacterial Agents; Cystatin C; Cystatins; Dipeptides; Drug Resistance, Multiple, Bacterial; Gram-Positive Cocci; Humans; Methicillin Resistance; Microbial Sensitivity Tests; Oligopeptides; Staphylococcus aureus; Streptococcus pyogenes; Journal Article; Research Support, Non-U.S. Gov't}},
  language     = {{eng}},
  number       = {{11}},
  pages        = {{1004--1010}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{APMIS : acta pathologica, microbiologica, et immunologica Scandinavica}},
  title        = {{New antimicrobial cystatin C-based peptide active against gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus and multiresistant coagulase-negative staphylococci}},
  url          = {{https://lup.lub.lu.se/search/files/3002204/623901.pdf}},
  doi          = {{10.1111/j.1600-0463.2003.t01-1-apm1111110.x}},
  volume       = {{111}},
  year         = {{2003}},
}