Abstract
As one of receptors of the acquired membrane, human salivary α‑amylase (HSA) plays an important role in the formation of caries. In vitro conditions, sorghum procyanidins (SPC) tetramer has a better inhibitory effect on the adhesion of Streptococcus mutans to hydroxyapatite than SPC-dimer and SPC-trimer. This study investigated the interaction mechanism between HSA and SPC-tetramer using spectroscopic techniques including fluorescence, UV–vis absorption, and circular dichroism (CD). Fluorescence data revealed that the fluorescence quenching of HSA by SPC-tetramer was a static quenching process, and that the SPC-tetramer was bound with HSA at the ratio of 1:1 in SPC-tetramer-protein complex. Meanwhile, the analysis of CD demonstrated that the conformation of HSA was altered in the presence of SPC-tetramer. The conformation changes of HSA might contribute to the reduction of the adhesion of cariogenic bacteria and finally decrease the occurrence of dental caries.
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