Peptides as Therapeutic Agents Against Lung Cancer
Poster Number
55
Faculty Mentor Name
Jianhua Ren, Polina Eidelberg, Jasmine Vargas
Research or Creativity Area
Natural Sciences
Abstract
Peptides are chains of amino acids strung together by peptide bonds. The process involves condensation and dehydration reactions along the carboxyl group of one amino acid and the amino group of another. There are 20 standard amino acids, which when linked together in sequence, form peptides and proteins. Peptides have different structures, giving rise to diverse biological functions and potential for targeted activity. They have emerged as powerful therapeutic agents in medicine due to their high specificity for targeting biomolecules. Previously identified mechanisms of action for eliminating cancer cells include disruption of extracellular conditions that favor tumor growth, patient immune system activation, and tumor cell metastasis inhibition. Additionally, peptides are suitable for therapeutics because they are less toxic than traditional cisplatin-based cancer treatment methods. The objective for making this peptide is to further research their capabilities as therapeutic agents against lung cancer. To make the peptide of interest, solid phase-peptide synthesis was utilized. Solid-phase peptide synthesis begins with the deprotection of rink-amide resin. The necessary amino acids are added one by one using coupling and deprotection steps. In between every coupling and deprotection step, the peptide is washed. After the desired amino acids are added, the peptide is cleaved to remove the resin. An important apparatus, the shaker, is used in the lab to agitate the reagents in the vessel. After cleavage, the peptide is purified with diethyl ether washes. Lastly, the peptide was frozen in liquid nitrogen and put on the lyophilizer overnight to undergo sublimation in preparation for mass spectrometry analysis using a TSQ Fortis Plus. The peptide was successfully synthesized and became an addition to a cumulative library of peptides. According to the MS data, the mass-to-charge ratio confirmed that the correct peptide sequence was made. The MS/MS data further supported that the correct sequence was made as several y and b fragments are seen in the data affirming this claim as well. This peptide will be used for future testing in lung cancer cell lines to see its effect in targeting specific mutated cells. Based on preliminary cell culture results, we anticipate that the peptide has therapeutic effects that can lead to potential cancer treatment in the future.
Location
University of the Pacific, DeRosa University Center
Start Date
26-4-2025 10:00 AM
End Date
26-4-2025 1:00 PM
Peptides as Therapeutic Agents Against Lung Cancer
University of the Pacific, DeRosa University Center
Peptides are chains of amino acids strung together by peptide bonds. The process involves condensation and dehydration reactions along the carboxyl group of one amino acid and the amino group of another. There are 20 standard amino acids, which when linked together in sequence, form peptides and proteins. Peptides have different structures, giving rise to diverse biological functions and potential for targeted activity. They have emerged as powerful therapeutic agents in medicine due to their high specificity for targeting biomolecules. Previously identified mechanisms of action for eliminating cancer cells include disruption of extracellular conditions that favor tumor growth, patient immune system activation, and tumor cell metastasis inhibition. Additionally, peptides are suitable for therapeutics because they are less toxic than traditional cisplatin-based cancer treatment methods. The objective for making this peptide is to further research their capabilities as therapeutic agents against lung cancer. To make the peptide of interest, solid phase-peptide synthesis was utilized. Solid-phase peptide synthesis begins with the deprotection of rink-amide resin. The necessary amino acids are added one by one using coupling and deprotection steps. In between every coupling and deprotection step, the peptide is washed. After the desired amino acids are added, the peptide is cleaved to remove the resin. An important apparatus, the shaker, is used in the lab to agitate the reagents in the vessel. After cleavage, the peptide is purified with diethyl ether washes. Lastly, the peptide was frozen in liquid nitrogen and put on the lyophilizer overnight to undergo sublimation in preparation for mass spectrometry analysis using a TSQ Fortis Plus. The peptide was successfully synthesized and became an addition to a cumulative library of peptides. According to the MS data, the mass-to-charge ratio confirmed that the correct peptide sequence was made. The MS/MS data further supported that the correct sequence was made as several y and b fragments are seen in the data affirming this claim as well. This peptide will be used for future testing in lung cancer cell lines to see its effect in targeting specific mutated cells. Based on preliminary cell culture results, we anticipate that the peptide has therapeutic effects that can lead to potential cancer treatment in the future.
