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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 ; Schalén, Claes LU and Grubb, Anders LU (2003) In APMIS : acta pathologica, microbiologica, et immunologica Scandinavica1988-01-01+01:00 111(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
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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 Scandinavica1988-01-01+01:00
volume
111
issue
11
pages
7 pages
publisher
John Wiley & Sons
external identifiers
  • pmid:14629266
  • wos:000187201300002
  • scopus:0346244038
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
2007-07-05 11:00:23
date last changed
2018-01-07 06:26:38
@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},
  keyword      = {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},
  series       = { APMIS : acta pathologica, microbiologica, et immunologica Scandinavica1988-01-01+01:00},
  title        = {New antimicrobial cystatin C-based peptide active against gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus and multiresistant coagulase-negative staphylococci},
  url          = {http://dx.doi.org/10.1111/j.1600-0463.2003.t01-1-apm1111110.x},
  volume       = {111},
  year         = {2003},
}