Solid Phase Peptide Synthesis of AC3 and CA3
Poster Number
20A
Research or Creativity Area
Natural Sciences
Abstract
Introduction:
Peptides are molecules made of two or more amino acids connected to one another by peptide bonds. The difference between peptides and proteins is that peptides are small, and consist of short a short chain of amino acids, while proteins are much larger. Synthetic peptides play significant roles in people’s everyday lives. Simply changing the position of the amino acids can have a drastic effect on the peptide’s properties. The focus of this research was on synthesizing short tetrapeptides containing cysteine and alanine, A3C, CA3, acetylated-A3C and acetylated-CA3. The acetyl group protects the N-terminus from ionization.
Method:
Peptides were synthesized using solid phase peptide synthesis. This procedure begins by adding rink amide resin to an SPPS vessel. The rink amide resin is used as the foundation or starting point for the peptide. The first step is an initial deprotection step; 20% piperidine in dimethylformamide (DMF) is used to remove the Fmoc protection group on the resin. After deprotection, the first amino acid is attached to the resin through the coupling, The coupling reagents include the amino acid along Hexafluorophosphate Benzotriazole Tetramethyl Uronium (HBTU) and N,N'-Diisopropylethylamine (DIPEA). The peptide is complete after several rounds of deprotection and coupling, and the peptide is acetylated, if needed. After every deprotection and coupling step, the peptide is washed with methanol (MeOH), Dichloromethane (DCM), and DMF to remove any excess reagents and impurities. Then the peptide is cleaved from the resin; the cleavage step also removes protecting groups on the side chains. After cleavage, the peptide goes through purification and lyophilization to remove any impurities.
Results/Conclusion:
The desired peptides were successfully synthesized. The sequence and purity were validated through mass spectrometry analysis on the LTQ-XL. The SPPS lab protocol can be applied to the synthesis of a variety of peptides. The peptides will be used for future studies on their thermochemical properties and reactivity by using mass spectrometry methods.
Location
Don and Karen DeRosa University Center (DUC) Poster Hall
Start Date
27-4-2024 10:30 AM
End Date
27-4-2024 12:30 PM
Solid Phase Peptide Synthesis of AC3 and CA3
Don and Karen DeRosa University Center (DUC) Poster Hall
Introduction:
Peptides are molecules made of two or more amino acids connected to one another by peptide bonds. The difference between peptides and proteins is that peptides are small, and consist of short a short chain of amino acids, while proteins are much larger. Synthetic peptides play significant roles in people’s everyday lives. Simply changing the position of the amino acids can have a drastic effect on the peptide’s properties. The focus of this research was on synthesizing short tetrapeptides containing cysteine and alanine, A3C, CA3, acetylated-A3C and acetylated-CA3. The acetyl group protects the N-terminus from ionization.
Method:
Peptides were synthesized using solid phase peptide synthesis. This procedure begins by adding rink amide resin to an SPPS vessel. The rink amide resin is used as the foundation or starting point for the peptide. The first step is an initial deprotection step; 20% piperidine in dimethylformamide (DMF) is used to remove the Fmoc protection group on the resin. After deprotection, the first amino acid is attached to the resin through the coupling, The coupling reagents include the amino acid along Hexafluorophosphate Benzotriazole Tetramethyl Uronium (HBTU) and N,N'-Diisopropylethylamine (DIPEA). The peptide is complete after several rounds of deprotection and coupling, and the peptide is acetylated, if needed. After every deprotection and coupling step, the peptide is washed with methanol (MeOH), Dichloromethane (DCM), and DMF to remove any excess reagents and impurities. Then the peptide is cleaved from the resin; the cleavage step also removes protecting groups on the side chains. After cleavage, the peptide goes through purification and lyophilization to remove any impurities.
Results/Conclusion:
The desired peptides were successfully synthesized. The sequence and purity were validated through mass spectrometry analysis on the LTQ-XL. The SPPS lab protocol can be applied to the synthesis of a variety of peptides. The peptides will be used for future studies on their thermochemical properties and reactivity by using mass spectrometry methods.
