New antimicrobial cystatin C-based peptide active against gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus and multiresistant coagulase-negative staphylococci
(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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- author
- Jasir, Aftab LU ; Kasprzykowski, Franciszek ; Kasprzykowska, Regina ; Lindström, Veronica LU ; Schalén, Claes LU and Grubb, Anders LU
- organization
- publishing date
- 2003-11
- 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}}, }