Peptide Bioregulators Based on IPH Complexes

Nutrition is one of the most crucial environmental factors that continuously influence the human body from birth to the very last moments of life. Food substances, as they transform into structural elements of the body’s cells through metabolism, provide physical and mental performance, determine human health, and impact the duration of life. Dietary disruptions always lead to various negative consequences. Therefore, rational and age-appropriate nutrition, considering one’s profession and health status, is viewed as a fundamental factor in preventing most human diseases, including cardiovascular (atherosclerosis, myocardial infarction, stroke, hypertension, etc.), oncological, gastrointestinal, metabolic disorders, and more.

Numerous studies indicate that one of the characteristics of the diet in economically developed countries in recent decades is the relatively high consumption of industrially processed food products. Such products typically undergo rigorous technological processing, leading to a significant reduction in their content of biologically active components: vitamins, minerals, and other bioactive substances that play a vital regulatory role in the metabolic processes of the human body, as well as in the functions of its individual organs and systems.

It is known that the regulatory systems of the intestine transport peptides formed during digestion from proteins significantly faster. This fact confirms the nutritional value of biologically active peptides obtained from food and their ability to coordinate the functioning of the body’s regulatory systems.

Currently, the role of peptides in forming compensatory-adaptive reactions of the body in response to stress and disturbances in homeostasis has been established. Peptides are considered promising agents for enhancing the resistance of the human body to extreme influences, preventing premature aging, and the development of age-related pathologies.

The study of the structural and functional features of these substances is of paramount importance in developing our understanding of the mechanisms of peptide action. This was noted as early as the beginning of the 20th century by the eminent Russian scientist Ivan Pavlov, who was awarded the Nobel Prize in 1904 for his work on the physiology of digestion.

Despite the multi-level hierarchy, all mechanisms regulating homeostasis share a common goal: coordinating the processes of biosynthesis and maintaining the genetic stability of the cellular composition of the body’s organs and tissues.

The process of peptide bioregulation of the structural and functional homeostasis of cell populations mediated by the action of endogenous regulatory peptides synthesized by various tissues of the body is well known. Disruption of peptide bioregulation reduces the body’s resistance to destabilizing factors in the external and internal environments, which is one of the causes of premature aging. In addition to this, there exists a physiological pathway for regulating various body functions, characterized by the fact that humans obtain proteins through food, which, under the action of gastric juice enzymes, break down into short peptides and amino acids. These compounds regulate the functions of the organs and systems for which they are specific.

Years of experimental research have shown that when exposed to adverse environmental factors, emotional stress, and the development of age-related pathologies, there is a disturbance in the process of self-regulation of the functions of the body’s main systems. This can be corrected by replenishing the deficient endogenous peptides.

A new approach to the prevention of age-related diseases and the restoration of impaired functions is bioregulatory therapy, which is based on the use of endogenous peptide bioregulators for both preventive and therapeutic purposes.

The foundation of bioregulatory therapy lies in the pathogenetic application of peptide bioregulators derived from the organs and tissues of animals in various diseases, pathological conditions, and aging. It is essential to study peptides with a known structure to advance our understanding of peptide regulation of aging.

Through the investigation of the breakdown of di-, tri-, and tetrapeptides in environments with varying pH levels and under the influence of stomach enzymes (proteases) and the proximal part of the small intestine, it has been determined that these preparations belong to the group of poorly hydrolyzable or resistant to hydrolysis peptides.

It has been found that the administration of peptides and peptide complexes with food to both male and female rats aged 3 months (young animals) and 11 months (mature animals) led to changes in the activity of digestive enzymes (sucrase, maltase, alkaline phosphatase, amino- and dipeptidases) responsible for the hydrolysis of carbohydrates, proteins, and phosphoric acid esters in different parts of the gastrointestinal tract (stomach, duodenum, jejunum, ileum, and colon). The most significant increase in enzyme activity was observed in animals aged 11 months, reducing the differences in enzyme activity levels among rats of different age groups. These findings indicate that short peptides IPH have a regulatory effect on the activity of gastrointestinal tract enzymes during aging.

The application of short peptides IPH and peptide complexes based on them for 21 days resulted in improvements in the transport characteristics of the small intestine in older rats. The results of the study of the impact of peptides on the activity of digestive enzymes and the absorption of glucose and glycine in the small intestine of older rats indicate that the enhancement of enzyme and transport system activity in the small intestine after peptide administration contributes to better food assimilation and the normalization of digestive function during aging.

As a result, a fundamentally new approach to the search for physiologically active peptides has been developed. Based on the analysis of the amino acid sequence of polypeptides, short di- and tripeptides containing 2 or 3 amino acids, which serve as the “active center” of IPH peptide complexes, have been identified. In terms of effectiveness, short peptides surpass preparations based on extracts and act in minimal doses. Experimental studies have shown that the composition and sequence of amino acids in the molecules of di- and tripeptides determine their biological properties. The study of short peptides IPH with established structures allows for a deep understanding of their mechanisms of action and the creation of a new high-tech class of parapharmaceuticals, dietary supplements, and sports nutrition products for optimizing the functions of the body’s major systems.

The process of protein synthesis occurs continuously in the body. When even one essential amino acid is lacking, protein synthesis is disrupted. This can lead to serious problems, from digestive disorders to depression and growth retardation. Individual amino acids, their derivatives, and products of metabolism serve as mediators of nerve endings, signals for communication with the external environment, inhibitors of specific biochemical reactions, act as adaptogens, and form the basis for the synthesis of regulatory peptides and hormones. The primary amino acid sequence contains the information necessary for protein formation.

It is known that to influence physiological processes, the presence of an entire protein molecule is not always necessary. Moreover, in some cases, fragments consisting of 2-4 amino acid residues are more effective than native compounds. Thus, the regulation and coordination of the body’s functions can be carried out through the cleavage of polypeptides, in which fragments with specific activity, specificity, and direction of action on various physiological systems are detached from sufficiently long chains depending on the body’s needs. Such cleavage also alters other properties of active molecules, such as hydrophobicity, which determines their ability to pass through cell membranes and histohematological barriers.

Experimental and clinical studies have been conducted to study this new class of drugs, allowing for the characterization of their specific activity and effectiveness in the restoration and maintenance of the functions of various organs and systems.

Sanitary-chemical studies have confirmed the complete absence of toxic elements and heavy metals in both finished forms and raw materials used in their production.

To confirm the safety of their clinical use, a study of general toxicity was conducted.

In studies of acute toxicity, it was found that the consumption of doses exceeding the therapeutic and clinically recommended doses, even by 5000 times, did not cause acute toxic reactions.

The study of subacute and chronic toxicity indicates the absence of side effects with their prolonged use in animals at doses exceeding therapeutic doses by 1000 times. When evaluating the general condition of animals, morphological and biochemical indicators of peripheral blood, the morphological state of internal organs, the condition of the cardiovascular and respiratory systems, liver and kidney function, no pathological changes in the animals’ bodies were found in studies of chronic toxicity.

Thus, the absence of general toxicity indicates the safety of clinical use of IPH peptide complexes for the purpose of optimizing the function of various organs and systems.