Inhibitory effects of carvacrol on glucansucrase from Streptococcus mutans and salivary α-amylase: in silico and in vitro studies

Basit Öğe Kaydı
dc.contributor.authorKocabay, Samet
dc.contributor.authorAlagoz, M. Abdullah
dc.contributor.authorAkkaya, Birnur
dc.date.accessioned2025-05-04T16:45:34Z
dc.date.available2025-05-04T16:45:34Z
dc.date.issued2025
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractBackground/aim: Streptococcus mutans produces glucansucrase, an enzyme that converts sucrose into lactic acid, which lowers the pH in the oral environment and leads to tooth enamel demineralization, a key factor in dental caries. Additionally, glucansucrase facilitates the formation of extracellular polysaccharides, which promote bacterial adhesion to tooth surfaces. This study investigates the inhibitory effects of carvacrol, a natural compound, on glucansucrase activity both in vitro and in silico. Materials and methods: Glucansucrase enzyme was purified from S. mutans. The inhibitory effects of carvacrol against glucansucrase enzyme were investigated both in vitro and in silico. Results: In the presence of 50 mM carvacrol, glucansucrase and salivary amylase activities were reduced by 51.25% and 14.85%, respectively. Carvacrol did not significantly inhibit (4.73%) the salivary amylase enzyme at 10 mM. Glucansucrase activity decreased by 51.63% in the presence of 10 mM acarbose, which was used as a positive control in glucansucrase enzyme studies. Acarbose inhibited salivary amylase with 82.54% loss of enzyme activity in the presence of 1 mM acarbose. The docking score obtained for carvacrol was -5.262 kcal/mol, while that obtained for acarbose was -6.084 kcal/mol. We carried out molecular dynamics simulation studies for 100 ns to determine the stability of carvacrol in the active site of the protein. Carvacrol demonstrated stable binding to glucansucrase with hydrogen bonds and interactions at key residues (ASP477, GLN960, and ASP909), confirmed by molecular dynamics simulations. Carvacrol remained stable between 16 and 100 ns. Conclusion: Carvacrol selectively inhibits glucansucrase without significantly affecting salivary amylase, making it a more targeted inhibitor compared to acarbose, which inhibits both enzymes. Docking studies indicated that while carvacrol has a lower binding affinity than acarbose, its stable interaction with the enzyme suggests sustained inhibitory action. These findings highlight carvacrol as a promising natural compound for preventing dental caries, offering a more selective alternative to traditional inhibitors. Further in vivo studies are necessary to assess its therapeutic efficacy and safety in clinical applications for oral health.
dc.description.sponsorshipScientific and Technological Research Council of Turkiye [221Z344, TUBIdot;TAK-1002-A]
dc.description.sponsorshipThis work (ID: 221Z344) was supported by The Scientific and Technological Research Council of Turkiye (TUB & Idot;TAK-1002-A).
dc.identifier.doi10.55730/1300-0152.2727
dc.identifier.issn1300-0152
dc.identifier.issn1303-6092
dc.identifier.issue1
dc.identifier.pmid40104578
dc.identifier.scopus2-s2.0-86000665152
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.55730/1300-0152.2727
dc.identifier.urihttps://hdl.handle.net/20.500.12418/35118
dc.identifier.volume49
dc.identifier.wosWOS:001470412300008
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTubitak Scientific & Technological Research Council Turkey
dc.relation.ispartofTurkish Journal of Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WOS_20250504
dc.subjectCarvacrol
dc.subjectglucansucrase
dc.subjectStreptococcus mutans
dc.subjectbiofilm
dc.subjectamylase
dc.titleInhibitory effects of carvacrol on glucansucrase from Streptococcus mutans and salivary α-amylase: in silico and in vitro studies
dc.typeArticle

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
PubMed İndeksli Yayınlar Koleksyonu
Scopus İndeksli Yayınlar Koleksiyonu