Title

Synthesis of biologically active tripeptide Arg- Gly-Asp (RGD).

Poster Number

7

Format

Poster Presentation

Abstract/Artist Statement

The short sequence like Arg-Gly-Asp (RGD) is primarily involved in protein binding on cell surfaces. Model studies using RGD and RGD-derived peptide are very important toward understanding the biological function of RGD-containing peptides. However RGD peptides are not easily available commercially. We synthesized the tripeptide RGD using solid-phase peptide synthesis (SPPS). The Wang Resin was used as the solid subport. The amino acids Asp, Gly and Arg were coupled to the Wang Resin, respectively. The coupling reagents used were diisoproplycarbodiimide (DIC) and 1- Hydroxybenzotriazole (HOBT). The amino acids used were protected with 9- fluorenylmethyloxycarbonyl (Fmoc) at the N-terminus. This N-terminus protecting group was removed by basic piperidine. An UV-Vis spectrophotometer was used to determine the progress of the deprotection reaction, for fmoc absorbs UV light at 301 nm. Once the entire peptide chain Arg-Gly-Asp was linked to the resin, the peptide was cleaved with Triflouroacetic acid (TFA). The solution obtained was concentrated with a rotovap. Chloroform extraction was performed to remove organic impurities. A crude peptide was obtained by removing the solvent using a centrifuge liked to a vacuum pump. The crude peptide was introduced in a mass spectrometer for MS/MS analysis.

Location

Pacific Geosciences Center

Start Date

24-4-2004 9:00 AM

End Date

24-4-2004 5:00 PM

This document is currently not available here.

Share

COinS
 
Apr 24th, 9:00 AM Apr 24th, 5:00 PM

Synthesis of biologically active tripeptide Arg- Gly-Asp (RGD).

Pacific Geosciences Center

The short sequence like Arg-Gly-Asp (RGD) is primarily involved in protein binding on cell surfaces. Model studies using RGD and RGD-derived peptide are very important toward understanding the biological function of RGD-containing peptides. However RGD peptides are not easily available commercially. We synthesized the tripeptide RGD using solid-phase peptide synthesis (SPPS). The Wang Resin was used as the solid subport. The amino acids Asp, Gly and Arg were coupled to the Wang Resin, respectively. The coupling reagents used were diisoproplycarbodiimide (DIC) and 1- Hydroxybenzotriazole (HOBT). The amino acids used were protected with 9- fluorenylmethyloxycarbonyl (Fmoc) at the N-terminus. This N-terminus protecting group was removed by basic piperidine. An UV-Vis spectrophotometer was used to determine the progress of the deprotection reaction, for fmoc absorbs UV light at 301 nm. Once the entire peptide chain Arg-Gly-Asp was linked to the resin, the peptide was cleaved with Triflouroacetic acid (TFA). The solution obtained was concentrated with a rotovap. Chloroform extraction was performed to remove organic impurities. A crude peptide was obtained by removing the solvent using a centrifuge liked to a vacuum pump. The crude peptide was introduced in a mass spectrometer for MS/MS analysis.