English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Antimicrobial peptides (AMPs) are anti-infectives that have potential as anovel and untapped class of biotherapeutics. Modes of action of antimicrobialpeptides imply interaction with cell envelope. Comprehensive understanding ofpeculiarities of interactions of antimicrobial peptides with cell envelope isnecessary to perform the task-oriented design of new biotherapeutics, againstwhich for microbes it is hard to work out resistance. In order to enable a denovo design with low costs and in high throughput, in silico predictive modelshave to be required. To develop the performant predictive model, comprehensiveknowledge on mechanisms of action of AMPs has to be possessed. The lastknowledge will allow us to encode amino acid sequences expressively and to getsuccess to the choosing of the accurate classifier of AMPs. A shared protectivelayer of microbial cells is inner, plasmatic membrane. The interaction of AMPwith a biological membrane (native and/or artificial) is the mostcomprehensively studied. We provide a review of mechanisms and results ofinteraction of AMP with the cell membrane, relying on the survey ofphysicochemical, aggregative and structural features of AMPs. Potency andmechanism of action of AMP have presented in the terms of amino acidcompositions and distributions of the polar and apolar residues along thechain, that is in such physicochemical features of peptides as thehydrophobicity, hydrophilicity, and amphiphilicity. Many different approacheswere used to classify AMPs. The survey of the knowledge on sequences,structures, and modes of actions of AMP, allows concluding that, only thephysicochemical features of AMPs give the capability to perform the unambiguousclassification. Comprehensive knowledge of physicochemical features of AMP isnecessary to develop task-oriented methods of design of peptide-basedantibiotics de novo.

Physicochemical Features and Peculiarities of Interaction of Antimicrobial Peptides with the Membrane