New antimicrobial peptide active against Gram-positive pathogens
Jasir, Aftab LU ; Kasprzykowski, F ; Lindström, Veronica LU
; Schalén, Claës
LU
and Grubb, Anders
LU
(2004)
In Indian Journal of Medical Research
119(Suppl.).
p.74-76
- Abstract
- Background & objectives: Human and animal cystatins have been shown to inhibit the replication of certain viruses and bacteria, though it is not directly demonstrated that the effects are due to protease inhibitory capacity of the cystatins. We report antibacterial properties of a novel antimicrobial peptidyl derivative, (2S)-2-(N-alpha-benzyloxycarbonyl-arginyl-leucylamido)-1-(E)-cinnamoyla mido-3-methylbutane, structurally based upon the aminoterminal segment of the inhibitory centre of the human cysteine protease inhibitor, cystatin C. Methods: Clinical isolates of group A, B, C and G streptococci were collected. The antibacterial activity of Cystapep 1 derivative was tested by agar well diffusion method. Results: Cystapep 1,... (More)
- Background & objectives: Human and animal cystatins have been shown to inhibit the replication of certain viruses and bacteria, though it is not directly demonstrated that the effects are due to protease inhibitory capacity of the cystatins. We report antibacterial properties of a novel antimicrobial peptidyl derivative, (2S)-2-(N-alpha-benzyloxycarbonyl-arginyl-leucylamido)-1-(E)-cinnamoyla mido-3-methylbutane, structurally based upon the aminoterminal segment of the inhibitory centre of the human cysteine protease inhibitor, cystatin C. Methods: Clinical isolates of group A, B, C and G streptococci were collected. The antibacterial activity of Cystapep 1 derivative was tested by agar well diffusion method. Results: Cystapep 1, displayed antibacterial activity against several clinically important Gram-positive bacteria. It displayed minimal inhibitory and bactericidal concentrations of about 16 mug/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. Interpretation & conclusion: Cystapep 1 also showed high activity against methicillin-resistant Staph. aureus (MRSA) and multi-antibiotic resistant coagulase negative staphylococci (CNS), suggesting its mechanism of action to be different from most currently used antibiotics. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/272832
- author
- Jasir, Aftab
LU
; Kasprzykowski, F
; Lindström, Veronica
LU
; Schalén, Claës
LU
and Grubb, Anders
LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Staphylococcus aureus, antimicrobial peptide, cystatin C, Streptococcus, pyogenes
- in
- Indian Journal of Medical Research
- volume
- 119
- issue
- Suppl.
- pages
- 74 - 76
- publisher
- Council Of Medical Research
- external identifiers
-
- pmid:15232166
- wos:000222679400017
- scopus:3442877866
- ISSN
- 0971-5916
- language
- English
- LU publication?
- yes
- id
- dfdc6eac-1d6e-4714-9481-1fd2176fc3d0 (old id 272832)
- alternative location
- http://www.icmr.nic.in/ijmr/ijmr_supp/15.pdf
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15232166&dopt=Abstract
- date added to LUP
- 2016-04-01 17:00:39
- date last changed
- 2023-01-05 04:31:37
@article{dfdc6eac-1d6e-4714-9481-1fd2176fc3d0,
abstract = {{Background & objectives: Human and animal cystatins have been shown to inhibit the replication of certain viruses and bacteria, though it is not directly demonstrated that the effects are due to protease inhibitory capacity of the cystatins. We report antibacterial properties of a novel antimicrobial peptidyl derivative, (2S)-2-(N-alpha-benzyloxycarbonyl-arginyl-leucylamido)-1-(E)-cinnamoyla mido-3-methylbutane, structurally based upon the aminoterminal segment of the inhibitory centre of the human cysteine protease inhibitor, cystatin C. Methods: Clinical isolates of group A, B, C and G streptococci were collected. The antibacterial activity of Cystapep 1 derivative was tested by agar well diffusion method. Results: Cystapep 1, displayed antibacterial activity against several clinically important Gram-positive bacteria. It displayed minimal inhibitory and bactericidal concentrations of about 16 mug/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. Interpretation & conclusion: Cystapep 1 also showed high activity against methicillin-resistant Staph. aureus (MRSA) and multi-antibiotic resistant coagulase negative staphylococci (CNS), suggesting its mechanism of action to be different from most currently used antibiotics.}},
author = {{Jasir, Aftab and Kasprzykowski, F and Lindström, Veronica and Schalén, Claës and Grubb, Anders}},
issn = {{0971-5916}},
keywords = {{Staphylococcus aureus; antimicrobial peptide; cystatin C; Streptococcus; pyogenes}},
language = {{eng}},
number = {{Suppl.}},
pages = {{74--76}},
publisher = {{Council Of Medical Research}},
series = {{Indian Journal of Medical Research}},
title = {{New antimicrobial peptide active against Gram-positive pathogens}},
url = {{http://www.icmr.nic.in/ijmr/ijmr_supp/15.pdf}},
volume = {{119}},
year = {{2004}},
}