Solid phase peptide synthesis and subsequent release from the solid support while retaining side chain protecting groups has grown in popularity. This strategy has been applied not only in the synthesis of proteins, enabling condensation of multiple protected peptide fragments but has also been implemented for the synthesis of peptides cyclized using head-to-tail cyclization strategies. While synthesis of the linear peptide precursor can be relatively straightforward, purification of the highly hydrophobic protected peptide can be challenging using standard reversed phased chromatography methods. Herein, we explore several strategies for the purification of fully protected synthetic peptides. We compare the relative efficiencies of several stationary phases commonly used in reversed phase chromatography and additionally the efficiency of normal phase chromatography as an alternative purification strategy.

Alternative strategies for purification of fully protected peptides using flash chromatography

254th National Meeting (2017)

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