Solid Phase Peptide Synthesis and Mass Spectrometry Analysis of AACAA & AAACA
Format
Poster Presentation
Faculty Mentor Name
Dr. Jianhua Ren
Faculty Mentor Department
Chemistry
Graduate Student Mentor Name
Yuntao Zhang
Graduate Student Mentor Department
Chemistry
Abstract/Artist Statement
Peptides are short chains of amino acids and many of them possess critical biological functions. For example, Glutathione is only three amino acids long but is the key antioxidant in all cells. Besides all their natural functionalities, peptides also play a significant role in pharmaceutical products. Peptides could interfere with protein-protein interactions, which are the foundation of cellular processes. By targeting receptors that activate pathways leading to disease, peptides can downregulate the expression of disease-associated protein interactions. To study their structure and reactivity, peptides could be synthesized in the laboratory using Solid Phase Peptide Synthesis (SPPS). In this research, two isomeric peptides were synthesized to study the cysteine position on their acidity and tendency of forming disulfide bonds.
Peptides AACAA and AAACA were synthesized using Solid Phase Peptide Synthesis (SPPS) with rink amide resin. The process includes a repetition of deprotection, coupling, and washing steps in between, allowing high efficiency attachment of one amino acid in each cycle. After reaching the target sequence, the peptides are cleaved off the resin and purified with precipitation and lyophilization. Mass spectrometry analysis was performed to check the identity and purity of the peptides.
The synthesis of peptides AACAA and AAACA were proven to be successful according to sample appearance and mass spectrometry analysis. Fragment ion values for each peptide were theoretically evaluated using the MS-product program in UCSF Protein Prospector. The observed ions that were emitted upon peptide fragmentation in the mass spectrometer matched our expected values, indicating successful synthesis of both peptides. The percent yields of peptides AACAA and AAACA were 63.8% and 56.6%, respectively.
Location
Virtual
Start Date
25-4-2020 1:00 PM
End Date
25-4-2020 3:00 PM
Solid Phase Peptide Synthesis and Mass Spectrometry Analysis of AACAA & AAACA
Virtual
Peptides are short chains of amino acids and many of them possess critical biological functions. For example, Glutathione is only three amino acids long but is the key antioxidant in all cells. Besides all their natural functionalities, peptides also play a significant role in pharmaceutical products. Peptides could interfere with protein-protein interactions, which are the foundation of cellular processes. By targeting receptors that activate pathways leading to disease, peptides can downregulate the expression of disease-associated protein interactions. To study their structure and reactivity, peptides could be synthesized in the laboratory using Solid Phase Peptide Synthesis (SPPS). In this research, two isomeric peptides were synthesized to study the cysteine position on their acidity and tendency of forming disulfide bonds.
Peptides AACAA and AAACA were synthesized using Solid Phase Peptide Synthesis (SPPS) with rink amide resin. The process includes a repetition of deprotection, coupling, and washing steps in between, allowing high efficiency attachment of one amino acid in each cycle. After reaching the target sequence, the peptides are cleaved off the resin and purified with precipitation and lyophilization. Mass spectrometry analysis was performed to check the identity and purity of the peptides.
The synthesis of peptides AACAA and AAACA were proven to be successful according to sample appearance and mass spectrometry analysis. Fragment ion values for each peptide were theoretically evaluated using the MS-product program in UCSF Protein Prospector. The observed ions that were emitted upon peptide fragmentation in the mass spectrometer matched our expected values, indicating successful synthesis of both peptides. The percent yields of peptides AACAA and AAACA were 63.8% and 56.6%, respectively.