Title

The Synthesis of Small Oligopeptides Containing Cysteine Residues

Poster Number

10C

Lead Author Major

Biochemistry

Lead Author Status

Junior

Second Author Major

Biochemistry

Second Author Status

Senior

Format

Poster Presentation

Faculty Mentor Name

Jianhua Ren

Faculty Mentor Email

jren@pacific.edu

Faculty Mentor Department

Chemistry

Graduate Student Mentor Name

Michael Browne

Graduate Student Mentor Email

m_browne1@u.pacific.edu

Graduate Student Mentor Department

Chemistry

Abstract/Artist Statement

In regard to polypeptides, cysteine residues are composed of a sidechain group containing a thiol group responsible for the formation of disulfide bonds, which are covalent bonds that consist of two thiol groups linked together. In biological systems, disulfide bonds are imperative to forming many secondary and tertiary protein structures. One particular enzyme known as thioredoxin serves to control where these bonds form and ultimately catalyze oxidative protein folding. Furthermore, many neurodegenerative diseases such as Alzheimer's and prions are linked to disulfide bond scrambling, which causes proteins to misfold. Research by our group has shown that the proximity of the cysteine residue with respect to the N-terminus and C-terminus is linked to the rate of which the disulfide bond forms. In order to understand the causes of different rates in disulfide bond formation, our lab has designed experiments to test the rates of disulfide formation among different peptides. Our research focuses on synthesizing small oligopeptides containing cysteine residues. The cysteine containing small oligopeptides were synthesized following the Solid Phase Peptide Synthesis protocol. This was done by linking amino acid residues together by beginning with the Rink Amide Resin through multiple rounds of deprotection, washing, coupling, and cleaving steps. The resulting peptides were purified by different techniques, followed by lyophilization, and confirmed through mass spectroscopy analysis. Overall, the main goal of our research is to synthesize small cysteine-containing peptides, analyze disulfide bonds between those small peptides, and to apply the findings to macro biological systems.

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

The Synthesis of Small Oligopeptides Containing Cysteine Residues

DeRosa University Center, Ballroom

In regard to polypeptides, cysteine residues are composed of a sidechain group containing a thiol group responsible for the formation of disulfide bonds, which are covalent bonds that consist of two thiol groups linked together. In biological systems, disulfide bonds are imperative to forming many secondary and tertiary protein structures. One particular enzyme known as thioredoxin serves to control where these bonds form and ultimately catalyze oxidative protein folding. Furthermore, many neurodegenerative diseases such as Alzheimer's and prions are linked to disulfide bond scrambling, which causes proteins to misfold. Research by our group has shown that the proximity of the cysteine residue with respect to the N-terminus and C-terminus is linked to the rate of which the disulfide bond forms. In order to understand the causes of different rates in disulfide bond formation, our lab has designed experiments to test the rates of disulfide formation among different peptides. Our research focuses on synthesizing small oligopeptides containing cysteine residues. The cysteine containing small oligopeptides were synthesized following the Solid Phase Peptide Synthesis protocol. This was done by linking amino acid residues together by beginning with the Rink Amide Resin through multiple rounds of deprotection, washing, coupling, and cleaving steps. The resulting peptides were purified by different techniques, followed by lyophilization, and confirmed through mass spectroscopy analysis. Overall, the main goal of our research is to synthesize small cysteine-containing peptides, analyze disulfide bonds between those small peptides, and to apply the findings to macro biological systems.