Solid Phase Peptide Synthesis

Poster Number

13B

Lead Author Major

Pre-Pharmacy

Lead Author Status

Junior

Second Author Major

Prep-Pharmacy

Second Author Status

Junior

Third Author Major

Biochemistry

Third Author Status

Junior

Fourth Author Major

Biochemistry

Fourth Author Status

Freshman

Format

Poster Presentation

Faculty Mentor Name

Jianhua Ren

Faculty Mentor Department

Chemistry

Graduate Student Mentor Name

Kim Harvey

Abstract/Artist Statement

Introduction:

A peptide is a molecule that consists of two or more amino acids and a chain of peptides makes up a protein. Peptides and proteins are fundamental to the human body and have many different functions depending on their sequence. Solid phase peptide synthesis (SPPS) was used to synthesize acetylated-CAG which consists of the amino acids cysteine, alanine, and glycine. The acetyl group affects the function of the peptide in biological processes. The purpose of studying certain sequences of amino acids is to expand our knowledge of peptides.

Method:

In SPPS, the entire reaction occurs in an SPPS vessel containing rink amide resin, which serves as a solid support for the peptide. The first step is deprotection, which involves using 20% piperidine in dimethylformamide (DMF) to remove the Fmoc protecting group from the amine group on the resin, which allows coupling to occur. Afterwards, the amino acids Fmoc-glycine, Fmoc-alanine, and Fmoc-cysteine were coupled one by one, a total of three coupling steps. The acetylation step involves the attachment of an acetyl group to the N-terminus of the peptide. The next step is cleavage, which removes the peptide from the resin. This is followed by purification, which removes any impurities in the peptide from the synthesis steps. After purification, the peptide is lyophilized which dries and further purifies the peptide, resulting in the dry, purified final product.

Results/Conclusion:

Following the procedure, Ac-CAG was successfully synthesized. The peptide sequence was confirmed by mass spectrometry analysis. The peptides will be used for future studies on their thermochemical properties and reactivity by using mass spectrometry methods.

Location

Information Commons, William Knox Holt Memorial Library and Learning Center

Start Date

29-4-2023 10:00 AM

End Date

29-4-2023 1:00 PM

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Apr 29th, 10:00 AM Apr 29th, 1:00 PM

Solid Phase Peptide Synthesis

Information Commons, William Knox Holt Memorial Library and Learning Center

Introduction:

A peptide is a molecule that consists of two or more amino acids and a chain of peptides makes up a protein. Peptides and proteins are fundamental to the human body and have many different functions depending on their sequence. Solid phase peptide synthesis (SPPS) was used to synthesize acetylated-CAG which consists of the amino acids cysteine, alanine, and glycine. The acetyl group affects the function of the peptide in biological processes. The purpose of studying certain sequences of amino acids is to expand our knowledge of peptides.

Method:

In SPPS, the entire reaction occurs in an SPPS vessel containing rink amide resin, which serves as a solid support for the peptide. The first step is deprotection, which involves using 20% piperidine in dimethylformamide (DMF) to remove the Fmoc protecting group from the amine group on the resin, which allows coupling to occur. Afterwards, the amino acids Fmoc-glycine, Fmoc-alanine, and Fmoc-cysteine were coupled one by one, a total of three coupling steps. The acetylation step involves the attachment of an acetyl group to the N-terminus of the peptide. The next step is cleavage, which removes the peptide from the resin. This is followed by purification, which removes any impurities in the peptide from the synthesis steps. After purification, the peptide is lyophilized which dries and further purifies the peptide, resulting in the dry, purified final product.

Results/Conclusion:

Following the procedure, Ac-CAG was successfully synthesized. The peptide sequence was confirmed by mass spectrometry analysis. The peptides will be used for future studies on their thermochemical properties and reactivity by using mass spectrometry methods.