Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.

@article{Ravi2015SupramolecularAF,
  title={Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.},
  author={Jascindra Ravi and Angelo Bella and Ana Jo{\~a}o V Correia and Baptiste Lamarre and Maxim G. Ryadnov},
  journal={Physical chemistry chemical physics : PCCP},
  year={2015},
  volume={17 24},
  pages={
          15608-14
        }
}
Host defence peptides (HDPs) are effector components of innate immunity that provide defence against pathogens. These are small-to-medium sized proteins which fold into amphipathic conformations toxic to microbial membranes. Here we explore the concept of supramolecular amphipathicity for probing antimicrobial propensity of HDPs using elementary HDP-like amphiphiles. Such amphiphiles are individually inactive, but when ordered into microscopic micellar assemblies, respond to membrane binding… 
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References

SHOWING 1-10 OF 30 REFERENCES

Ultrashort antibacterial and antifungal lipopeptides

The simple composition of these lipopeptides and their diverse specificities should make them economically available, innate immunity-mimicking antimicrobial and antifungal compounds for various applications.

Anti-antimicrobial Peptides

Using sequences from native helical families such as cathelicidins, cecropins, and magainins, it is demonstrated that designed antagonists can co-fold with antimicrobial peptides into functionally inert helical oligomers.

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

It is shown that pores formed by antimicrobial peptides in supported lipid bilayers are not necessarily limited to a particular diameter, nor they are transient, but can expand laterally at the nano-to-micrometer scale to the point of complete membrane disintegration.

Designing antimicrobial peptides: form follows function

Multidrug-resistant bacteria are a severe threat to public health. Conventional antibiotics are becoming increasingly ineffective as a result of resistance, and it is imperative to find new…

Antimicrobial peptides of multicellular organisms

Multicellular organisms live, by and large, harmoniously with microbes. The cornea of the eye of an animal is almost always free of signs of infection. The insect flourishes without lymphocytes or…

Membrane mediated regulation in free peptides of HIV-1 gp41: minimal modulation of the hemifusion phase.

It is shown that these peptides interact locally without the conformational support of helical heptad repeat regions in native gp41 and that the modulation is not mutual with the FPP peptide operating as a primary regulator of the MPE-FPP interactions in the hemifusion phase.

Measuring the forces involved in polyvalent adhesion of uropathogenic Escherichia coli to mannose-presenting surfaces.

An experimental procedure that measures the forces of adhesion resulting from the interaction of uropathogenic Escherichia coli to molecularly well defined models of cellular surfaces and suggests that the combination of optical tweezers and appropriately functionalized SAMs is a uniquely synergistic system with which to study polyvalent adhesion of bacteria to biologically relevant surfaces.

Antimicrobial properties of amyloid peptides.

At least one human antimicrobial peptide, protegrin-1, which kills microbes by a channel-forming mechanism, has been shown to possess the ability to form extended amyloid fibrils very similar to those of classic disease-forming amyloids.

Cicada-inspired cell-instructive nanopatterned arrays

The surfaces engineered in this study are titania (TiO2) nanowire arrays that are selectively bactericidal against motile bacteria, while capable of guiding mammalian cell proliferation according to the type of the array.

Combinatorial discovery of polymers resistant to bacterial attachment

A group of structurally related materials comprising ester and cyclic hydrocarbon moieties that substantially reduced the attachment of pathogenic bacteria (Pseudomonas aeruginosa, Staphylococcus aureus and Escherichia coli) are identified.