Lyophilization

Last Friday (January 17th), I returned to RPI to work more with samples from a peptide synthesis. Today, we went through the process of lyophilization, also known as freeze-drying. The peptide samples were from a synthesis that JP completed earlier, which were already frozen in the freezer. To prepare the peptides for lyophilization, we used liquid nitrogen to freeze the peptides and then covered the tubes with both parafilm and foil. We had to poke holes in the foil and parafilm with a thumbtack for the process to work properly. In the process of lyophilization, we use a machine like the one shown below.

In the process of lyophilization, the peptide tubes are placed in a canister that attaches to one of the spouts of the machine. Inside the center pole of the machine, there is an extremely cold coil that's even colder than the liquid nitrogen. This machine applies both force and extremely cold temperatures to the peptides. As the peptides slowly melt, the pressure causes the water vapor to be transferred to the colder coil, where it condenses. After two or three days, this process eventually removes all of the water from the peptide samples, leaving them freeze-dried with the appearance like a dried sponge or old chewing gum. Lyophilization allows us to turn the peptide samples into a powder, which will be used in future experiments with our synthesized peptides.

Today, we also discussed possible topics for a my own research project. My project will likely have to do with testing blocking buffer solutions. My first task was to check the pH of SYPRO protein gel stain to make sure it's not too acidic to use with peptide microarrays. Using pH strips, I found the pH to be approximately 5.

 I will provide more details of my project in coming weeks. This week, I am tasked with researching details about different blocking buffer solutions that are currently in use. I can't wait to establish the objectives of my project!