Abstract
Fibronectin (Fn) is a multifunctional adhesive protein found on cell surfaces as well as in plasma. It is also believed to play an important role in bacterial adherence to host tissues. Molecular analyses of Fn have shown that the amino acid triplet arginine-glycine-aspartic acid (RGD) sequence functions as a binding site. We examined the role of the RGD sequence on bacterial adherence to Fn. The pretreatment of Streptococcus mitis with synthetic RGD-containing peptide reduced the number of bound bacteria to the Fn coated plates by 76%. In contrast, a control peptide containing the RGE sequence showed no inhibition. These data indicate that synthetic RGD peptides may be useful for the inhibition of bacterial adherence to Fn on host cell surfaces.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: The Journal of Nihon University School of Dentistry
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
