Studies have been conducted to evaluate the antitumorigenic activity of peptides isolated from enzymatic hydrolysate of cow colostrum. The colostrum peptides were studied by a MALDI-TOPH mass spectrometer, decryption was carried out using the Mascot database, option was the Peptide Fingerprint ("Matrix Science", USA) using the Protein NCBI database. As a model object, cell lines C6 (ATCC CCL-107) were used, the range of which did not exceed 15 at the time of experimental work, and HEK 293T (ATCCCRL-3216), the passage of which did not exceed 20 at the time of experimental work. The following values of the concentrations of the studied samples were used as standard values: 500; 400; 300; 200; 100; 50 mcg/ml. As a negative control, cells were used to which individual peptides were not added. During the experiment, C6 cells were placed in a 96-well tablet in the amount of 10,000 cells per well. The studied peptides (RR1, TT3, mpR1, mpT, RR4, T1.1) were added to the cells. When using the RR1 peptide, the population of the C6 cell line decreases by 50 % after 48 hours. The minimum concentration of the peptide RR1, at which 50 % of tumor cells die in 48 hours, is 351.7 mcg/ml (reliability of the result: R2 = 0.7217). The antitumorigenic peptide RR1 consists of 8 amino acids and has a molecular weight of 9.0 kDa. In the known proteomic databases, the isolated peptide RR1 from cow colostrum is absent, accordingly, its biological functions have not been studied. It was found that an isoelectric point of the studied peptide sample is in a strongly alkaline medium – 10.63 and does not depend on the predominance of amine or carboxyl groups in the peptide composition. For the peptide RR1, the hydrophilicity value was 18.57 Kcal∙mol-1. The 3D model of the studied peptide allowed us to establish that it had low chemical activity since its charge was +2.

Tikhonov Sergey L., Tikhonova Natalia V.

1. Chakrabarti S., Guha S., Majumder K. Food-derived bioactive peptides in human health: challenges and opportunities. Nutrients, 2018; 10: 1738.
2. Reshetnik E. I., Utochkina E. A. Healty food products with probiotic and prebiotic properties. Foods and Raw Materials, 2013; 1; 1: 88–94.
3. Ivankina I. F., Reshetnik E. I., Frolova N. A. Funktsional'naya pishchevaya dobavka vtorichnogo syr'ya pantovogo olenevodstva dlya obogashcheniya konditerskikh izdelii [Functional food additive secondary raw antler deerraising for enrichment confectionery]. Dal'nevostochnyi agrarnyi vestnik. – Far Eastern Agrarian Bulletin, 2013; 4: 50–52. (in Russ.).
4. Reshetnik E. I., Utochkina E. A. Vliyanie komponentnogo sostava na pishchevuyu i biologicheskuyu tsennost' produkta [Infuence of component composition on food and biological value of a combination product]. Vestnik Vostochno-Sibirskogo gosudarstvennogo universiteta tekhnologij i upravleniya. – Bulletin of the East Siberian State University of Technology and Management, 2013; 2: 63–67. (in Russ.).
5. Xiang X. W., Zheng H. Z., Wang R., Chen H., Xiao J.-X., Zheng B. Ameliorative effects of peptides derived from oyster (Crassostrea gigas) on immunomodulatory function and gut microbiota structure in cyclophosphamide-treated mice. Marine Drugs, 2021; 19: 456.
6. Rajendran S. R., Ejike C. E., Gong M., Hannah W., Udenigwe C. C. Preclinical evidence on the anticancer properties of food peptides. Protein and Peptide Letters, 2017; 24: 126–136.
7. Blanco-Miguez A., Gutierrez-Jacome A., Perez-Perez M., Perez-Rodriguez G., Catalan-Garcia S., Fdez-Riverola F. [et al.]. From amino acid sequence to bioactivity: The biomedical potential of antitumor peptides. Protein Sciences, 2016; 25: 1084–1095.
8. Deslouches B., Di Y. P. Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications. Oncotarget, 2017; 8: 46635–46651.
9. Raucher D. Tumor targeting peptides: novel therapeutic strategies in glioblastoma. Current Opinion in Pharmacology, 2019; 47: 9–14.
10. Sani M. A, Separovic F. How membrane-active peptides get into lipid membranes. Accounts of Chemical Research, 2016; 49: 1130–8.
11. Zhao H., Qin X., Yang D., Jiang Y., Zheng W., Wang D. [et al.]. The development of activatable lytic peptides for targeting triple negative breast cancer. Cell Death Discovery, 2017;3: 1–8.
12. Cook K. L., Metheny-Barlow L. J., Tallant E. A., Gallagher P. E. Angiotensin (1–7) reduces fibrosis in orthotopic breast tumors. Canadian Research, 2010; 70: 8319–28.
13. Accardo A., Tesauro D., Morelli G. Peptide-based targeting strategies for simultaneous imaging and therapy with nanovectors. Polymer Journal, 2013: 45: 481–93.
14. Marqus S., Pirogova E., Piva T. J. Evaluation of the use of therapeutic peptides for cancer treatment. Journal of Biomedical Science, 2017; 24: 1–15.
15. Ruiwu L., Xiaocen L., Wenwu X., Kit S. Tumor-targeting peptides from combinatorial libraries. Advanced Drug Delivery Reviews, 2017; 110–111: 13–37.