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Melittin alcalase-hydrolysate: a novel chemically characterized multifunctional bioagent; antibacterial, anti-biofilm and anticancer
Department of Zoology and Entomology, Faculty of Science, Al-Azhar University (Girls), Nasr City, Egypt.
Department of Botany and Microbiology, Faculty of Science, Al-Azhar University (Boys), Cairo, Egypt.
Department of Botany and Microbiology, Faculty of Science, Al-Azhar University (Boys), Cairo, Egypt.
Protein Research Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), City of Scientific Research and Technological Applications (SRTA-City), New Borg Al-Arab City, A, lexandria, Egypt; Pharmaceutical and Fermentation Industries Development Center, City of Scientific Research and Technological Applications (SRTA-City), New Borg Al-Arab City, Alexandria, Egypt; Pharos University in Alexandria, Alexandria, Egypt.
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2024 (English)In: Frontiers in Microbiology, E-ISSN 1664-302X, Vol. 15, article id 1419917Article in journal (Refereed) Published
Abstract [en]

The prevalent life-threatening microbial and cancer diseases and lack of effective pharmaceutical therapies created the need for new molecules with antimicrobial and anticancer potential. Bee venom (BV) was collected from honeybee workers, and melittin (NM) was extracted from BV and analyzed by urea-polyacrylamide gel electrophoresis (urea-PAGE). The isolated melittin was hydrolyzed with alcalase into new bioactive peptides and evaluated for their antimicrobial and anticancer activity. Gel filtration chromatography fractionated melittin hydrolysate (HM) into three significant fractions (F1, F2, and F3), that were characterized by electrospray ionization mass spectrometry (ESI-MS) and evaluated for their antimicrobial, anti-biofilm, antitumor, and anti-migration activities. All the tested peptides showed antimicrobial and anti-biofilm activities against Gram-positive and Gram-negative bacteria. Melittin and its fractions significantly inhibited the proliferation of two types of cancer cells (Huh-7 and HCT 116). Yet, melittin and its fractions did not affect the viability of normal human lung Wi-38 cells. The IC50 and selectivity index data evidenced the superiority of melittin peptide fractions over intact melittin. Melittin enzymatic hydrolysate is a promising novel product with high potential as an antibacterial and anticancer agent.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2024. Vol. 15, article id 1419917
Keywords [en]
antibacterial activity, anticancer activity, Apis mellifera, bee venom, electro-spray ionization, enzymatic hydrolysis, melittin, wound healing assay
National Category
Biochemistry and Molecular Biology Physical Chemistry
Identifiers
URN: urn:nbn:se:umu:diva-228425DOI: 10.3389/fmicb.2024.1419917ISI: 001282524700001PubMedID: 39091304Scopus ID: 2-s2.0-85200235378OAI: oai:DiVA.org:umu-228425DiVA, id: diva2:1889258
Funder
Region VästerbottenLions Cancerforskningsfond i NorrThe Kempe FoundationsAvailable from: 2024-08-15 Created: 2024-08-15 Last updated: 2024-08-15Bibliographically approved

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Khalil, Ali OsmanSitohy, Basel

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