vetpressАграрная наукаAgrarian science0869-81552686-701XРедакция журнала "Аграрная наука"10.32634/0869-8155-2024-381-4-132-137vetpress-3037Research ArticleАГРОИНЖЕНЕРИЯ И ПИЩЕВЫЕ ТЕХНОЛОГИИAGROENGINEERING AND FOOD TECHNOLOGIESНовый антимикробный пищевой пептид: характеристика, свойства и оценка эффективностиA new antimicrobial food peptide: characteristics, properties and effectiveness evaluationhttps://orcid.org/0009-0006-8660-4527УлитинаЕ. А.UlitinaE. A.

Елизавета Андреевна Улитина, аспирант 

ул. Карла Либкнехта, 42, Екатеринбург, 620075

Elizaveta Andreevna Ulitina, Postgraduate Student 

 

   

egorulitin@inbox.ruВалиеваШ. С.ValievaSh. S.

Шолпан Сергеевна Валиева, аспирант

ул. Карла Либкнехта, 42, Екатеринбург, 620075

Sholpan Sergeevna Valieva, Postgraduate Student

42 Karl Liebknecht Str., Yekaterinburg, 620075

   

sholpan.v85@gmail.comhttps://orcid.org/0000-0003-4863-9834ТихоновС. Л.TikhonovS. L. 

Сергей Леонидович Тихонов, доктор технических наук, профессор

ул. Карла Либкнехта, 42, Екатеринбург, 620075

Сибирский тракт, 37, Екатеринбург, 620100

Sergey Leonidovich Tikhonov, Doctor of Technical Sciences, Professor

42 Karl Liebknecht Str., Yekaterinburg, 620075

37 Siberian Tract, Yekaterinburg, 620100

tihonov75@bk.ruhttps://orcid.org/0000-0001-5841-1791ТихоноваН. В.TikhonovaN.  V.

Наталья Валерьевна Тихонова, доктор технических наук, профессор

ул. Карла Либкнехта, 42, Екатеринбург, 620075

Natalia Valeryevna Tikhonova, Doctor of Technical Sciences, Professor

42 Karl Liebknecht Str., Yekaterinburg, 620075

   

tihonov75@bk.ruУральский государственный аграрный исследовательский университетРоссияUral State Agrarian UniversityRussian FederationУральский государственный аграрный исследовательский университет; Уральский государственный лесотехнический университетРоссияUral State Agrarian University; Ural State Forestry Engineering UniversityRussian Federation20242504202404132137Copyright © Улитина Е.А., Валиева Ш.С., Тихонов С.Л., Тихонова Н.В., 20242024Улитина Е.А., Валиева Ш.С., Тихонов С.Л., Тихонова Н.В.Ulitina E.A., Valieva S.S., Tikhonov S.L., Tikhonova N.V.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.vetpress.ru/jour/article/view/3037

Перспективными кандидатами в качестве противобактериальных препаратов являются антимикробные пептиды (АМП), присутствующие в молозиве коров.

Цели исследований — выделение, теоретическое обоснование и подтверждение биологической активности нового АМП из пепсинового гидролизата молозива коров с аминокислотной последовательностью EKLAKNKLARGLKRK. По базе данных Protein NCBI, выделенный АМП, идентифицируется как AW655195.1 105840 MARC 1BOV / Bos taurus (крупный рогатый скот). При идентификации АМП по базе данных антимикробных пептидов APD он не найден. При идентификации АМП по базе данных DRAMP исследуемый объект отсутствует, но по характеристикам относится к классу противомикробных. Общее гидрофобное соотношение пептида, определенное APD, составляет 33%. Общий чистый заряд равен +6, молекулярная масса составляет 1753,151 Да. Потенциал связывания с белками (индекс Бомана) на уровне 3,44 ккал/моль. Выделенный АМП по характеристикам близок к известным, включенным в базу данных APD. АМП относится к катионным гидрофобным α-спиральным, что предполагает его противомикробную активность. В результате экспериментов in vitro доказана противомикробная и противоопухолевая активность пептида.

Promising candidates as antibacterial drugs are antimicrobial peptides (AMP) present in cow colostrum. The aim of the research is to isolate, theoretically substantiate and confirm the biological activity of a new AMP from pepsin hydrolysate of cow colostrum with the amino acid sequence EKLAKNKLARGLKRK. According to the Protein NCBI database, the isolated AMP is identified as AW655195.1 105840 MARC 1BOV/ Bos taurus (cattle). When identifying AMP from the database of antimicrobial peptides APD, it was not found. When identifying AMP using the DRAMP database, the object under study is missing, but its characteristics belong to the antimicrobial class. The total hydrophobic ratio of the peptide determined by APD is 33%. The total net charge is +6, the molecular weight is 1753.151 Da. Protein binding potential (Boman index) at 3.44 kcal/mol. The selected AMP is close in characteristics to the known ones included in the APD database. AMP belongs to the cationic hydrophobic α-helical, which suggests its antimicrobial activity. As a result of in vitro experiments, the antimicrobial and antitumor activity of the peptide has been proven.

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The authors declare that there are no conflicts of interest present.