Title

An Overview of Synthesis and Identification of Peptides

Poster Number

10

Format

Poster Presentation

Abstract/Artist Statement

As part of ongoing projects, short peptides including Cys-Gly-Gly-Gly (CGGG) and Arg-Gly- Asp-Val (RGDV) were synthesized using the method of Solid Phase Peptide Synthesis (SPPS). First, an initial coupling of Fmoc-protected amino acid to the resin of choice was carried out. After deprotecting the N-terminus of the first amino acid, further coupling and deprotecting steps were systematically completed in a peptide synthesis vessel continually agitated by an automatic shaker, until the peptide chain of desired composition was attained. The peptide was then cleaved from the resin with a cleavage cocktail of varying composition, depending on peptide identity. The peptide-containing solution was next subjected to the low pressure of a rotovap that concentrated the peptide, preparing it for chloroform extraction and subsequent centrifugation under a vacuum pump. Successful synthesis of peptides was confirmed when sample obtained (in gel-like form) was identified, using fragmentation analyses based on MS/MS spectra from the Electrospray Ionization Triple Quadrupole Mass Spectrometer (ESI-3Q).The two peptides synthesized are of specific interest to us. Synthesized CGGG will be further analyzed for its chemical properties before utilizing it as a reference in studies on C(A)n helical peptides. RGD is known to have biological significance in protein binding with cell membranes, so our study of tetrapeptide RGDV may lend insight into how this occurs.

Location

Callison Hall

Start Date

6-5-2006 10:00 AM

End Date

6-5-2006 12:00 PM

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May 6th, 10:00 AM May 6th, 12:00 PM

An Overview of Synthesis and Identification of Peptides

Callison Hall

As part of ongoing projects, short peptides including Cys-Gly-Gly-Gly (CGGG) and Arg-Gly- Asp-Val (RGDV) were synthesized using the method of Solid Phase Peptide Synthesis (SPPS). First, an initial coupling of Fmoc-protected amino acid to the resin of choice was carried out. After deprotecting the N-terminus of the first amino acid, further coupling and deprotecting steps were systematically completed in a peptide synthesis vessel continually agitated by an automatic shaker, until the peptide chain of desired composition was attained. The peptide was then cleaved from the resin with a cleavage cocktail of varying composition, depending on peptide identity. The peptide-containing solution was next subjected to the low pressure of a rotovap that concentrated the peptide, preparing it for chloroform extraction and subsequent centrifugation under a vacuum pump. Successful synthesis of peptides was confirmed when sample obtained (in gel-like form) was identified, using fragmentation analyses based on MS/MS spectra from the Electrospray Ionization Triple Quadrupole Mass Spectrometer (ESI-3Q).The two peptides synthesized are of specific interest to us. Synthesized CGGG will be further analyzed for its chemical properties before utilizing it as a reference in studies on C(A)n helical peptides. RGD is known to have biological significance in protein binding with cell membranes, so our study of tetrapeptide RGDV may lend insight into how this occurs.