A microcalorimetric method to determine antimicrobial effects of two bile acid derivatives on Staphylococcus aureus

2011 ◽  
Vol 108 (3) ◽  
pp. 1293-1301
Author(s):  
Xingfeng Li ◽  
Cheng Jin ◽  
Wei Liu ◽  
Jian Zhou ◽  
Weijun Kong ◽  
...  
1983 ◽  
Vol 29 (12) ◽  
pp. 1653-1660 ◽  
Author(s):  
Toshichika Ohtomo

In a previous paper, we showed that bile acid derivatives inhibit capsule formation as well as taurine biosynthesis in a taurine+ (Tau+) encapsulated strain of Staphylococcus aureus. In the present study, binding of [14C]cholic acid ([14C]CA) and [14C]taurocholic acid ([14C]TA) to the staphylococcal polysaccharide antigen (SPA) of the capsular fraction was examined. The bile acids were found to bind with SPA via taurine of the Tau+ cells. [14C]CA bound with the SPA fraction of the Tau+ strain within 10–30 min, whereas 60–120 min was required in the binding of [14C]TA. Various bile acids competed with cholic acid binding to Tau+ cells which was shown by the inhibition of binding with cholic acid or taurocholic acid but not with glycholic acid. Binding of bile acid derivatives to a Tau− encapsulated mutant or to capsular material from this mutant was not observed.


2010 ◽  
Vol 179 (1-3) ◽  
pp. 742-747 ◽  
Author(s):  
Weijun Kong ◽  
Cheng Jin ◽  
Xiaohe Xiao ◽  
Yanling Zhao ◽  
Zulun Li ◽  
...  

2004 ◽  
Vol 15 (24) ◽  
pp. 3831-3833 ◽  
Author(s):  
Olga Bortolini ◽  
Giancarlo Fantin ◽  
Marco Fogagnolo ◽  
Lara Mari

2022 ◽  
Vol 23 (1) ◽  
pp. 524
Author(s):  
Sergey V. Kravchenko ◽  
Pavel A. Domnin ◽  
Sergei Y. Grishin ◽  
Alexander V. Panfilov ◽  
Viacheslav N. Azev ◽  
...  

The need to develop new antimicrobial peptides is due to the high resistance of pathogenic bacteria to traditional antibiotics now and in the future. The creation of synthetic peptide constructs is a common and successful approach to the development of new antimicrobial peptides. In this work, we use a simple, flexible, and scalable technique to create hybrid antimicrobial peptides containing amyloidogenic regions of the ribosomal S1 protein from Staphylococcus aureus. While the cell-penetrating peptide allows the peptide to enter the bacterial cell, the amyloidogenic site provides an antimicrobial effect by coaggregating with functional bacterial proteins. We have demonstrated the antimicrobial effects of the R23F, R23DI, and R23EI hybrid peptides against Staphylococcus aureus, methicillin-resistant S. aureus (MRSA), Pseudomonas aeruginosa, Escherichia coli, and Bacillus cereus. R23F, R23DI, and R23EI can be used as antimicrobial peptides against Gram-positive and Gram-negative bacteria resistant to traditional antibiotics.


ARKIVOC ◽  
2006 ◽  
Vol 2006 (6) ◽  
pp. 40-48 ◽  
Author(s):  
O. Bortolini ◽  
G. Fantin ◽  
M. Fogagnolo ◽  
S. Maietti

2009 ◽  
Vol 239 (1) ◽  
pp. 21-28 ◽  
Author(s):  
Elisa Herraez ◽  
Rocio I.R. Macias ◽  
Jose Vazquez-Tato ◽  
Carlos Hierro ◽  
Maria J. Monte ◽  
...  

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