Group of Peptide Chemistry

Peptides and their derivatives are widely used in biology as molecular tools. Some peptides and peptidomimetics are used in medicine. Therefore, the development of effective peptide synthesis methods is a subject of ongoing research worldwide.


The Peptide Chemistry Group research is focused on the search of side reaction products that are formed during the actual steps of the chemical synthesis of peptide and peptidomimetics. Upon the identification of the products of new side reactions, the conditions for the chemical transformations are developed aiming to eliminate the formation of side products discovered. An inrease of an efficacy of a peptide synthesis method is expected as an applied result of the research.

  1. Development of methodology and elaboration of biologically-active peptides (peptidomimetics) chemical synthesis methods.

  2. Development of methodology of selective bioconjugation of synthetic peptides with biopharmaceuticals

  3. Investigation of structure-activity relationships of biologically-active peptide analogs

  1. Efficient chemical synthesis of the amide form of HLDF-6 peptide was developed.

  2. A new side reaction of NIn-formyl protecting group transfer to Nα is discovered. The reaction conditions aiming to minimize the formation of N-For truncated side products are suggested.

  3. A chemical method for the preparation of ketomethylene pseudopeptides was developed.

All publications (show selected)


Viatcheslav Azev

Preparation of active pharmaceutical ingridient based on Nα-acetyl C-amide terminal form of HLDF-6 peptide using optimized synthetic method

In collaboration with Laboratory of hormonal regulation proteins

Standard solid phase methods could not be applied for the preparation of the API samples due to the fact that current SPPS methodologies are still imperfect. Therfore, fragment condensation in solution method was developed, optimized and used for the preparation of the amide form of HLDF-6 peptide. That material could be purified and acetylated under the conditions where peptide salts of weak acids are acylated with variuos weak electrophilic derivatives of acetic acid including active esters and azolides. Appliaction of the acetylation reaction conditions described provides API samples in high yield and purity


  1. Zolotarev YuA, Dadayan AK, Kozik VS, Shram SI, Nagaev IYu, Azev VN, Bogachouk AP, Lipkin VM, Myasoedov NF (2019). Proteolytic Hydrolysis of the Antitumor Peptide HLDF-6-AA in Blood Plasma. Russ. J. Bioorganic Chem. 45 (5), 347–352

Development of efficient solid-phase synthesis methods for the preparation of peptides that possess immunosuppresive activity

In collaboration with Laboratory of Biological Testing,  Laboratory of pharmacokinetics

The relative efficacies of several synthesis methods have been investigated aiming to prepare target peptides that are quite potent in a test for suppression of the experimental autoimmune encephalomyelitis. Toward this goal chemical yields of the target peptides as well as side product distributions in the samples of the peptides obtained using various methods have been evaluated and quantitatively characterized. A variation of Fmoc/tBu methodology have been found to be the most efficient providing targets peptides in the highest chemical yield since it allowed to use a broader range of  activated amino acid derivatives. Side products of the amino acid doubling were detected among the side products of chemical synthesis. Some of the amino acid doubling side products made the HPLC purification step to be complicated. Nevertheless the synthetic methods developed allowed the preparation of the target peptides in sufficient quantities.

Development of peptide drugs for the treatment of multiple sclerosis

In collaboration with Laboratory of hormonal regulation proteins,  Laboratory of Biological Testing,  Laboratory of pharmacokinetics

Multiple sclerosis is a chronic autoimmune disease with neurological pathology. The dominant role of immunological processes in the development of the disease dictates the need for medications that specifically minimize the activity of immune processes. The peptides A8AMS and mA8AMS, homologous to the fragment of the human IgG VH domain, have been shown to act in vitro and in vivo, effectively reducing the symptoms of experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis. The results provide new opportunities for the development of peptide drugs for the treatment of multiple sclerosis.