scholarly journals Identification of duck liver-expressed antimicrobial peptide 2 and characterization of its bactericidal activity

2019 ◽  
Vol 32 (7) ◽  
pp. 1052-1061 ◽  
Author(s):  
Yeojin Hong ◽  
Anh Duc Truong ◽  
Janggeun Lee ◽  
Kyungbaek Lee ◽  
Geun-Bae Kim ◽  
...  
Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1140
Author(s):  
Silvana Alfei ◽  
Gabriella Piatti ◽  
Debora Caviglia ◽  
Anna Maria Schito

The growing resistance of bacteria to current chemotherapy is a global concern that urgently requires new and effective antimicrobial agents, aimed at curing untreatable infection, reducing unacceptable healthcare costs and human mortality. Cationic polymers, that mimic antimicrobial cationic peptides, represent promising broad-spectrum agents, being less susceptible to develop resistance than low molecular weight antibiotics. We, thus, designed, and herein report, the synthesis and physicochemical characterization of a water-soluble cationic copolymer (P5), obtained by copolymerizing the laboratory-made monomer 4-ammoniumbuthylstyrene hydrochloride with di-methyl-acrylamide as uncharged diluent. The antibacterial activity of P5 was assessed against several multi-drug-resistant clinical isolates of both Gram-positive and Gram-negative species. Except for strains characterized by modifications of the membrane charge, most of the tested isolates were sensible to the new molecule. P5 showed remarkable antibacterial activity against several isolates of genera Enterococcus, Staphylococcus, Pseudomonas, Klebsiella, and against Escherichia coli, Acinetobacter baumannii and Stenotrophomonas maltophilia, displaying a minimum MIC value of 3.15 µM. In time-killing and turbidimetric studies, P5 displayed a rapid non-lytic bactericidal activity. Due to its water-solubility and wide bactericidal spectrum, P5 could represent a promising novel agent capable of overcoming severe infections sustained by bacteria resistant the presently available antibiotics.


Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 421
Author(s):  
Areetha R. D’Souza ◽  
Matthew R. Necelis ◽  
Alona Kulesha ◽  
Gregory A. Caputo ◽  
Olga V. Makhlynets

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.


2010 ◽  
Vol 43 (4) ◽  
pp. 1198-1203 ◽  
Author(s):  
Patrícia da Silva Malheiros ◽  
Yasmine Miguel Serafini Micheletto ◽  
Nádya Pesce da Silveira ◽  
Adriano Brandelli

2009 ◽  
Vol 45 (5) ◽  
pp. 401-409 ◽  
Author(s):  
ROBERT J. VAN ABEL ◽  
YI-QUAN TANG ◽  
V.S.V. RAO ◽  
CRAIG H. DOBBS ◽  
DAT TRAN ◽  
...  

1996 ◽  
Vol 40 (8) ◽  
pp. 1941-1944 ◽  
Author(s):  
M E Klepser ◽  
M A Banevicius ◽  
R Quintiliani ◽  
C H Nightingale

Kill curves were determined for five isolates of Bacteroides fragilis with clindamycin at concentrations equal to the MIC or to 4, 16, and 64 times the MIC. Examination of plots of log CFU per milliliter versus time revealed no association between the clindamycin concentration and the rate and extent of the bactericidal activity against B. fragilis at or below 64 times the MIC.


2007 ◽  
Vol 31 (12) ◽  
pp. 1297-1309 ◽  
Author(s):  
Pinwen Peter Chiou ◽  
Chun-Mean Lin ◽  
Niels C. Bols ◽  
Thomas T. Chen

2003 ◽  
Vol 270 (4) ◽  
pp. 675-686 ◽  
Author(s):  
Noriaki Iijima ◽  
Norio Tanimoto ◽  
Yohko Emoto ◽  
Yohko Morita ◽  
Kazumasa Uematsu ◽  
...  

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