C. M. Nasadyuk

Danylo Halytsky Lviv National Medical University,
Department of Biochemistry, Lviv, Ukraine;
e-mail: nasadyukch@gmail.com

Received: 09 March 2021; Accepted: 22 September 2021

According to modern knowledge, the biological effect of many peptides is mediated by their short-chain fragments – oligopeptides – ranging from 2 to 20 amino acids and the activity of short peptides often significantly exceeds the activity of the peptide precursor. Aim of the review was to summarize the uptodate data on the stability of short peptide sequences, mechanisms of cell penetration, interaction with cell receptors, biological effects and approaches to clinical application. Stability of short peptides is mediated by their structure and molecular weight. Some di-/tripeptides were reported to be able to permeate through intestinal membranes in their intact forms via peptide transporter systems, while others are vulnerable to protease degradation. Although pinocytosis is presumed to be the main mechanism how short peptide sequences enter the cell, some lipophilic oligopeptides were shown to penetrate the cell membrane by the same mechanism as steroid or thyroid hormones and specific extracellular receptors were also described. Low-weighing oligopeptides realize their effect on the cell, chromosomal, genome and molecular levels. The advantages of oligopeptides include oral availability (for low weight compounds), low immunogenicity, high tissue specifici­ty, faster biological effect, better cost efficiency and environmental friendliness of their synthesis. Hence, short peptide sequences are regarded as promising candidates for pharmacotherapy, cell cultures and drug delivery­ purposes.