Manual Synthesis of Polypeptides
Poster Number
43
Format
Poster Presentation
Faculty Mentor Name
Jianhua Ren
Faculty Mentor Department
Chemistry
Abstract/Artist Statement
Polypeptides are small chains of amino acid monomers linked together by peptide bonds, which can then be linked together to create longer chains known as polymers or proteins. Enzymes are extremely intricate and complicated structures. They are so complicated that it is highly difficult to study their configuration and function. In place of enzymes, these peptides are used as a substitute to the active site of the enzymes to allow further research to be made. The method known as Solid Phase Peptide Synthesis (SPPS) was used to synthetically make peptides in a laboratory setting. This method requires repeated cycles of deprotection and coupling steps in order to expand the length of the synthesized peptide on a resin such as Rink Amide. Other reactions such as acetylation can be done to further specify the polypeptide. The peptide is then cleaved from the resin using a cleaving reagent. Multiple washing cycles and a final lyophilization were completed to continuously purify the product. A mass spectrometer is used to confirm the identity of the finished product by a full scan and a MS/MS scan. Examples of polypeptides formed include DGG, GGD, Ac-AAAK, Ac-KAAA.
Location
DeRosa University Center, Ballroom
Start Date
26-4-2014 2:00 PM
End Date
26-4-2014 4:00 PM
Manual Synthesis of Polypeptides
DeRosa University Center, Ballroom
Polypeptides are small chains of amino acid monomers linked together by peptide bonds, which can then be linked together to create longer chains known as polymers or proteins. Enzymes are extremely intricate and complicated structures. They are so complicated that it is highly difficult to study their configuration and function. In place of enzymes, these peptides are used as a substitute to the active site of the enzymes to allow further research to be made. The method known as Solid Phase Peptide Synthesis (SPPS) was used to synthetically make peptides in a laboratory setting. This method requires repeated cycles of deprotection and coupling steps in order to expand the length of the synthesized peptide on a resin such as Rink Amide. Other reactions such as acetylation can be done to further specify the polypeptide. The peptide is then cleaved from the resin using a cleaving reagent. Multiple washing cycles and a final lyophilization were completed to continuously purify the product. A mass spectrometer is used to confirm the identity of the finished product by a full scan and a MS/MS scan. Examples of polypeptides formed include DGG, GGD, Ac-AAAK, Ac-KAAA.