Solid Phase Peptide Synthesis and Mass Spectrometry analysis Ac3-P3-D
Poster Number
10B
Format
Poster Presentation
Faculty Mentor Name
Jianhua Ren
Faculty Mentor Department
Chemistry
Graduate Student Mentor Name
Yadwinder Singh Mann
Graduate Student Mentor Department
Chemistry
Abstract/Artist Statement
The polyproline peptides are of particular interest as they are known to exist in two helical forms, the polyproline I and polyproline II. In solution, The PPII helix is a left-handed helix, with three residues per turn, while PPI helix is a more tightly wound right-handed helix with 3.3 residues per turn. The ultimate goal of our research is to find the gas phase conformation of polyproline peptide by measuring the gas phase acidity using mass spectrometry methods and molecular modelling. In a series of investigation, we have synthesized Ac-P3D using solid-phase peptide synthesis (SPS), a method in which peptides are synthesized sequentially on a resin. The carboxyl terminus of the first peptide, aspartic acid, was first anchored to a resin bead. The Fmoc protecting group in the N-terminus of aspartic acid was then removed (deprotected) to allow for the attachment of the next amino acid, proline. Each coupling process was repeated with the addition of two more proline residues. The end step of our synthesis was acetylation in order to simulate the environment of proteins inside the body. After cleavage of the peptide from the resin, the peptide was purified using lyophilization. Finally the mass spectrometer was used to analyze the identity and sequence of the peptide.
Location
DeRosa University Center, Ballroom
Start Date
28-4-2018 1:00 PM
End Date
28-4-2018 3:00 PM
Solid Phase Peptide Synthesis and Mass Spectrometry analysis Ac3-P3-D
DeRosa University Center, Ballroom
The polyproline peptides are of particular interest as they are known to exist in two helical forms, the polyproline I and polyproline II. In solution, The PPII helix is a left-handed helix, with three residues per turn, while PPI helix is a more tightly wound right-handed helix with 3.3 residues per turn. The ultimate goal of our research is to find the gas phase conformation of polyproline peptide by measuring the gas phase acidity using mass spectrometry methods and molecular modelling. In a series of investigation, we have synthesized Ac-P3D using solid-phase peptide synthesis (SPS), a method in which peptides are synthesized sequentially on a resin. The carboxyl terminus of the first peptide, aspartic acid, was first anchored to a resin bead. The Fmoc protecting group in the N-terminus of aspartic acid was then removed (deprotected) to allow for the attachment of the next amino acid, proline. Each coupling process was repeated with the addition of two more proline residues. The end step of our synthesis was acetylation in order to simulate the environment of proteins inside the body. After cleavage of the peptide from the resin, the peptide was purified using lyophilization. Finally the mass spectrometer was used to analyze the identity and sequence of the peptide.