ABSTRACT
Background: This research sought to assess the impact of polyhexamethylene guanidine hydrochloride (PHMGH) and 1,3,5-triacryloyl hexahydro-1,3,5-triazine (TAT) on the antibacterial activity of an experimental resin sealant. Materials and Methods: The two experimental sealants were formulated based on previous research, and Streptococcus mutans (S. mutans) was tested for biofilm and planktonic bacteria's antibacterial properties. In 48 hours, 300 L of frozen S. mutans in skim milk was stored in an oven at 37°C in a microaerophilic atmosphere with 5% of CO2 and put on a petri plate containing brain-heart infusion (BHI) broth with agar at 15 g/L. By combining 100 mL of the subculture broth with 900 mL of a sterile saline solution (0.9%) in an Eppendorf tube, the initial inoculum used for the experiments was evaluated. The colonies were measured in colony-forming units per milliliter (CFU/mL) after being counted visually. To measure the antibacterial activity, log CFU/mL was used to express the number of bacteria in the broth that had been in contact with the samples for 24 hours. Results: Outcomes of antibacterial activity against planktonic bacteria and against biofilm development on polymerized materials. The two innovative sealant materials were found to differ significantly from one another, while group 2's mean and standard deviation values were larger. Conclusion: Dental sealants designed with PHMGH and TCPTAT for anticaries application showed less bacterial growth throughout time the cavity prevention properties of the resin sealant.
ABSTRACT
Neutralizing antibodies have become an important tool in treating infectious diseases. Recently, two separate approaches yielded successful antibody treatments for Ebola-one from genetically humanized mice and the other from a human survivor. Here, we describe parallel efforts using both humanized mice and convalescent patients to generate antibodies against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein, which yielded a large collection of fully human antibodies that were characterized for binding, neutralization, and three-dimensional structure. On the basis of these criteria, we selected pairs of highly potent individual antibodies that simultaneously bind the receptor binding domain of the spike protein, thereby providing ideal partners for a therapeutic antibody cocktail that aims to decrease the potential for virus escape mutants that might arise in response to selective pressure from a single-antibody treatment.
