Solid Phase Peptide Synthesis
Poster Number
7B
Research or Creativity Area
Natural Sciences
Abstract
PURCC Abstract Spring 2024
Title: Solid Phase Peptide Synthesis
Authors: Seung Ham, Wiley Winkler, Kevin Hahn
Introduction:
Peptides, essential molecular compounds composed of amino acids, serve as the building blocks of proteins that are vital for the functioning of the human body. With distinct sequences that dictate their function, they play a crucial role in the growth, repair, and maintenance of cells. The focus of the research was on the synthesis of the peptide sequences GAC and CAG. The letters GAC represent the amino acids: Glycine, Alanine, and Cysteine, which were selected specifically for their properties and structure. Through the selection of these peptide sequences, we sought to investigate their prospective functions in cellular processes as well as explore their roles in various biomedical applications.
Method:
Solid Phase Peptide Synthesis (SPPS) was employed to synthesize these peptides. In this method, the C-terminal amino acid is directly attached to resin beads, allowing for the controlled assembly of the peptide. Each amino acid has an Fmoc protecting group on the α-amino group, which prevents unwanted side reactions and ensures selective coupling. The deprotection step removes this protecting group, and the coupling steps add the amino acid to the peptide. In this way, peptides are synthesized from the N-terminus to the C-terminus. Following the coupling steps, the cleavage step releases the synthesized peptide from the solid resin. After cleavage, purification and lyophilization is carried out to remove impurities from the final peptide product. Finally, the percent yield of the peptide was calculated.
Result:
By following this procedure, the desired two tripeptides were successfully synthesized and their purity was evaluated by mass spectrometry. The peptides will be used for future studies on their thermochemical properties and reactivity by using mass spectrometry methods.
Location
Don and Karen DeRosa University Center (DUC) Poster Hall
Start Date
27-4-2024 10:30 AM
End Date
27-4-2024 12:30 PM
Solid Phase Peptide Synthesis
Don and Karen DeRosa University Center (DUC) Poster Hall
PURCC Abstract Spring 2024
Title: Solid Phase Peptide Synthesis
Authors: Seung Ham, Wiley Winkler, Kevin Hahn
Introduction:
Peptides, essential molecular compounds composed of amino acids, serve as the building blocks of proteins that are vital for the functioning of the human body. With distinct sequences that dictate their function, they play a crucial role in the growth, repair, and maintenance of cells. The focus of the research was on the synthesis of the peptide sequences GAC and CAG. The letters GAC represent the amino acids: Glycine, Alanine, and Cysteine, which were selected specifically for their properties and structure. Through the selection of these peptide sequences, we sought to investigate their prospective functions in cellular processes as well as explore their roles in various biomedical applications.
Method:
Solid Phase Peptide Synthesis (SPPS) was employed to synthesize these peptides. In this method, the C-terminal amino acid is directly attached to resin beads, allowing for the controlled assembly of the peptide. Each amino acid has an Fmoc protecting group on the α-amino group, which prevents unwanted side reactions and ensures selective coupling. The deprotection step removes this protecting group, and the coupling steps add the amino acid to the peptide. In this way, peptides are synthesized from the N-terminus to the C-terminus. Following the coupling steps, the cleavage step releases the synthesized peptide from the solid resin. After cleavage, purification and lyophilization is carried out to remove impurities from the final peptide product. Finally, the percent yield of the peptide was calculated.
Result:
By following this procedure, the desired two tripeptides were successfully synthesized and their purity was evaluated by mass spectrometry. The peptides will be used for future studies on their thermochemical properties and reactivity by using mass spectrometry methods.
