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Development of the new antimicrobial agents against antibiotic resistancepathogens is the nowadays challenge. Antimicrobial peptides (AMP) occur asimportant defence agents in many organisms and offer a viable alternative toconventional antibiotics. Therefore they have become increasingly recognized incurrent research as templates for prospective antibiotic agents. The efficientdesigning of the new antimicrobials on the basis of antimicrobial peptidesrequires comprehensive knowledge on those general physical-chemicalcharacteristics which allow to differ antimicrobial peptides from non-activeagainst microbs ones. According to supposed mechanisms of action, AMP interactwith and physically disrupt the bacterial membranes. Consequently,hydrophobicity, amphiphilicity and intrinsic aggregation propensities areconsidered as such major characteristics of the peptide, which determine theresults of peptide-membrane interactions. For some kind of peptides suchcharacteristics as hydrophobicity, amphiphilicity and aggregation biasdetermines their ability to compose transmembrane domain of the membraneprotein, whilst for others the same properties are respond for theirantimicrpobial activity, i.e. give them ability of membrane permeability andits damage. In this review we analyze the data about hydrophobicity,amphiphilicity and intrinsic aggregation propensities available in literaturein order to compare antimicrobial and transmembrane peptides and show what isthe common and what is the difference in this respect between them.

Transmembrane and Antimicrobial Peptides. Hydrophobicity, Amphiphilicity and Propensity to Aggregation