scholarly journals Effect of the Head-Group Geometry of Amino Acid-Based Cationic Surfactants on Interaction with Plasmid DNA

2008 ◽  
Vol 9 (7) ◽  
pp. 1852-1859 ◽  
Author(s):  
Vaibhav Jadhav ◽  
Souvik Maiti ◽  
Antara Dasgupta ◽  
Prasanta Kumar Das ◽  
Rita S. Dias ◽  
...  
Author(s):  
Bernat Pi-Boleda ◽  
Sravani Ramisetty ◽  
Ona Illa ◽  
Vicenç Branchadell ◽  
Rita S. Dias ◽  
...  

2021 ◽  
Vol 22 (7) ◽  
pp. 3299
Author(s):  
Damian Neubauer ◽  
Maciej Jaśkiewicz ◽  
Marta Bauer ◽  
Agata Olejniczak-Kęder ◽  
Emilia Sikorska ◽  
...  

Ultrashort cationic lipopeptides (USCLs) and gemini cationic surfactants are classes of potent antimicrobials. Our recent study has shown that the branching and shortening of the fatty acids chains with the simultaneous addition of a hydrophobic N-terminal amino acid in USCLs result in compounds with enhanced selectivity. Here, this approach was introduced into arginine-rich gemini cationic surfactants. L-cystine diamide and L-lysine amide linkers were used as spacers. Antimicrobial activity against planktonic and biofilm cultures of ESKAPE (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Enterobacter spp.) strains and Candida sp. as well as hemolytic and cytotoxic activities were examined. Moreover, antimicrobial activity in the presence of human serum and the ability to form micelles were evaluated. Membrane permeabilization study, serum stability assay, and molecular dynamics were performed. Generally, critical aggregation concentration was linearly correlated with hydrophobicity. Gemini surfactants were more active than the parent USCLs, and they turned out to be selective antimicrobial agents with relatively low hemolytic and cytotoxic activities. Geminis with the L-cystine diamide spacer seem to be less cytotoxic than their L-lysine amide counterparts, but they exhibited lower antibiofilm and antimicrobial activities in serum. In some cases, geminis with branched fatty acid chains and N-terminal hydrophobic amino acid resides exhibited enhanced selectivity to pathogens over human cells.


1995 ◽  
Vol 42 (2) ◽  
pp. 233-239 ◽  
Author(s):  
A Szalewska-Pałasz ◽  
G Wegrzyn

Replication of lambda plasmid DNA is halted in amino acid-starved wild type (stringent) strains whereas it proceeds in relA (relaxed) mutants. The only transcription which could be important in lambda plasmid DNA replication in amino acid-starved Escherichia coli cells is that starting from the pR promoter. Using a fusion which consists of the lacZ gene under the control of bacteriophage lambda pR promoter we found that transcription starting from this promoter was inhibited during the stringent, but not the relaxed, response in E. coli. We confirmed our conclusion by estimating the relative level of the pR transcript by RNA-DNA hybridization. We propose that decreased transcription from the pR promoter which serves as transcriptional activation of ori lambda is responsible for inhibition of lambda plasmid replication during the stringent response. The results presented in this paper, combined with our recent findings (published elsewhere), indicate that the transcriptional activation of ori lambda may be a main regulatory process controlling lambda DNA replication not only during the relaxed response but also in normal growth conditions.


Author(s):  
Mohammad Rashidi-Alavijeh ◽  
Soheila Javadian ◽  
Hussein Gharibi ◽  
Morteza Moradi ◽  
Ali Reza Tehrani-Bagha ◽  
...  

2008 ◽  
Vol 191 (4) ◽  
pp. 1126-1131 ◽  
Author(s):  
Alena Dabrazhynetskaya ◽  
Therese Brendler ◽  
Xinhua Ji ◽  
Stuart Austin

ABSTRACT The P1, P7, and pMT1 par systems are members of the P1 par family of plasmid partition elements. Each has a ParA ATPase and a ParB protein that recognizes the parS partition site of its own plasmid type to promote the active segregation of the plasmid DNA to daughter cells. ParB contacts two parS motifs known as BoxA and BoxB, the latter of which determines species specificity. We found that the substitution of a single orthologous amino acid in ParB for that of a different species has major effects on the specificity of recognition. A single change in ParB can cause a complete switch in recognition specificity to that of another species or can abolish specificity. Specificity changes do not necessarily correlate with changes in the gross DNA binding properties of the protein. Molecular modeling suggests that species specificity is determined by the capacity to form a hydrogen bond between ParB residue 288 and the second base in the BoxB sequence. As changes in just one ParB residue and one BoxB base can alter species specificity, plasmids may use such simple changes to evolve new species rapidly.


2016 ◽  
Vol 4 (48) ◽  
pp. 8025-8032 ◽  
Author(s):  
D. Sirisha Janni ◽  
U. Chandrasekhar Reddy ◽  
Soumya Saroj ◽  
K. M. Muraleedharan

The self-assembly of non-ionic amphiphiles with hydroxylated oxanorbornane head-group was controlled using amino acid units as spacers between hydrophilic and lipophilic domains to get spherical supramolecular aggregates suitable for drug delivery applications.


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