Title

Solid Phase Peptide Synthesis and Mass Spectrometry analysis Ac3-P3-D

Poster Number

10B

Lead Author Major

Biochemistry

Lead Author Status

Sophomore

Second Author Major

Pre-Dentistry

Second Author Status

Sophomore

Format

Poster Presentation

Faculty Mentor Name

Jianhua Ren

Faculty Mentor Email

jren@pacific.edu

Faculty Mentor Department

Chemistry

Graduate Student Mentor Name

Yadwinder Singh Mann

Graduate Student Mentor Email

y_mann@u.pacific.edu

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

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Apr 28th, 1:00 PM Apr 28th, 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.