scholarly journals Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation

2016 ◽  
Vol 17 (4) ◽  
pp. 552 ◽  
Author(s):  
David Pulido ◽  
Javier Arranz-Trullén ◽  
Guillem Prats-Ejarque ◽  
Diego Velázquez ◽  
Marc Torrent ◽  
...  
Keyword(s):  
Mechanism Of Action ◽  
Bacterial Cell ◽  
Membrane Permeation ◽  
Structural Determinants ◽  
Cell Agglutination ◽  
Antimicrobial Mechanism

Multivalent Nanofibers of a Controlled Length: Regulation of Bacterial Cell Agglutination

2012 ◽  
Vol 134 (36) ◽  
pp. 14722-14725 ◽  
Author(s):  
Dong-Woo Lee ◽  
Taehoon Kim ◽  
Il-Soo Park ◽  
Zhegang Huang ◽  
Myongsoo Lee
Keyword(s):  
Bacterial Cell ◽  
Cell Agglutination ◽  
Length Regulation

Supramolecular self-assemblies for bacterial cell agglutination driven by directional charge-transfer interactions

2018 ◽  
Vol 54 (23) ◽  
pp. 2922-2925 ◽  
Author(s):  
Dan Wu ◽  
Jie Shen ◽  
Hongzhen Bai ◽  
Guocan Yu
Keyword(s):  
Charge Transfer ◽  
Bacterial Cell ◽  
Cell Agglutination ◽  
E Coli ◽  
A Cell ◽  
Multivalent Interactions ◽  
Supramolecular Amphiphiles

Two supramolecular amphiphiles are fabricated through directional charge-transfer interactions, which self-assemble into nanofibers and nanoribbons. Due to the existence of galactose on their surface, these self-assemblies act as a cell glue to agglutinate E. coli, benefiting from multivalent interactions.

scholarly journals Real-Time Characterization of an Antimicrobial Mechanism-of-Action with Nonlinear Optical Scattering

2017 ◽  
Vol 112 (3) ◽  
pp. 382a
Author(s):  
Michael J. Wilhelm ◽  
Bruk Mensa ◽  
Mohammad Sharifian Gh. ◽  
William F. DeGrado ◽  
Hai-Lung Dai
Keyword(s):  
Real Time ◽  
Mechanism Of Action ◽  
Nonlinear Optical ◽  
Optical Scattering ◽  
Antimicrobial Mechanism

Monocyclic β -Lactam: A Review on Synthesis and Potential Biological Activities of a Multitarget Core

2020 ◽  
Vol 20 (16) ◽  
pp. 1653-1682
Author(s):  
Taíse H.O. Leite ◽  
Mauricio F. Saraiva ◽  
Alessandra C. Pinheiro ◽  
Marcus Vinícius N. de Souza
Keyword(s):  
Cell Wall ◽  
Organic Synthesis ◽  
Mechanism Of Action ◽  
Bacterial Cell ◽  
Bacterial Resistance ◽  
Biological Activities ◽  
Cell Wall Biosynthesis ◽  
Vast Number ◽  
Structural Modifications ◽  
New Compounds

A monocyclic ring in their structure characterizes monobactams, a subclass of β-lactam antibiotics. Many of these compounds have a bactericidal mechanism of action and acts as penicillin and cephalosporins, interfering with bacterial cell wall biosynthesis. The synthesis of novel β-lactams is an emerging area of organic synthesis research due to the problem of increasing bacterial resistance to existing β -lactam antibiotics, and, in this way, new compounds have been presented with several structural modifications, aiming to improve biological activities. Among the biological activities studied, the most outstanding are antibacterial, antitubercular, anticholesterolemic, anticancer, antiinflammatory, antiviral, and anti-enzymatic, among others. This review explores the vast number of works related to monocyclic β-lactams, compounds of great importance in scientific research.

Carbon Nanotube/Biocompatible Bola-Amphiphile Supramolecular Biohybrid Materials: Preparation and Their Application in Bacterial Cell Agglutination

2013 ◽  
Vol 25 (44) ◽  
pp. 6373-6379 ◽  
Author(s):  
Guocan Yu ◽  
Jinying Li ◽  
Wei Yu ◽  
Chengyou Han ◽  
Zhengwei Mao ◽  
...  
Keyword(s):  
Carbon Nanotube ◽  
Bacterial Cell ◽  
Cell Agglutination ◽  
Materials Preparation

Protein post-translational modification in host defense: the antimicrobial mechanism of action of human eosinophil cationic protein native forms

FEBS Journal ◽  
2014 ◽  
Vol 281 (24) ◽  
pp. 5432-5446 ◽  
Author(s):  
Vivian A. Salazar ◽  
Jenny Rubin ◽  
Mohammed Moussaoui ◽  
David Pulido ◽  
Maria Victòria Nogués ◽  
...  
Keyword(s):  
Host Defense ◽  
Mechanism Of Action ◽  
Eosinophil Cationic Protein ◽  
Post Translational Modification ◽  
Cationic Protein ◽  
Human Eosinophil ◽  
Antimicrobial Mechanism

scholarly journals Self-Assembling Peptide Dendron Nanoparticles with High Stability and a Multimodal Antimicrobial Mechanism of Action

ACS Nano ◽  
2021 ◽  
Author(s):  
Zhenheng Lai ◽  
Qiao Jian ◽  
Guoyu Li ◽  
Changxuan Shao ◽  
Yongjie Zhu ◽  
...  
Keyword(s):  
Mechanism Of Action ◽  
High Stability ◽  
Self Assembling ◽  
Antimicrobial Mechanism

scholarly journals Antimicrobial Action and Cell Agglutination by the Eosinophil Cationic Protein Are Modulated by the Cell Wall Lipopolysaccharide Structure

2012 ◽  
Vol 56 (5) ◽  
pp. 2378-2385 ◽  
Author(s):  
David Pulido ◽  
Mohammed Moussaoui ◽  
David Andreu ◽  
M. Victòria Nogués ◽  
Marc Torrent ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mechanism Of Action ◽  
Bacterial Infections ◽  
Eosinophil Cationic Protein ◽  
Antimicrobial Action ◽  
Protein Activity ◽  
Cationic Protein ◽  
Cell Agglutination ◽  
Content Type ◽  
Bacterial Agglutination

ABSTRACTAntimicrobial proteins and peptides (AMPs) are essential effectors of innate immunity, acting as a first line of defense against bacterial infections. Many AMPs exhibit high affinity for cell wall structures such as lipopolysaccharide (LPS), a potent endotoxin able to induce sepsis. Hence, understanding how AMPs can interact with and neutralize LPS endotoxin is of special relevance for human health. Eosinophil cationic protein (ECP) is an eosinophil secreted protein with high activity against both Gram-negative and Gram-positive bacteria. ECP has a remarkable affinity for LPS and a distinctive agglutinating activity. By using a battery of LPS-truncatedE. colimutant strains, we demonstrate that the polysaccharide moiety of LPS is essential for ECP-mediated bacterial agglutination, thereby modulating its antimicrobial action. The mechanism of action of ECP at the bacterial surface is drastically affected by the LPS structure and in particular by its polysaccharide moiety. We have also analyzed an N-terminal fragment that retains the whole protein activity and displays similar cell agglutination behavior. Conversely, a fragment with further minimization of the antimicrobial domain, though retaining the antimicrobial capacity, significantly loses its agglutinating activity, exhibiting a different mechanism of action which is not dependent on the LPS composition. The results highlight the correlation between the protein's antimicrobial activity and its ability to interact with the LPS outer layer and promote bacterial agglutination.

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