Amyloid-β as a “Difficult Sequence” in Solid Phase Peptide Synthesis

Title: Amyloid-β as a “Difficult Sequence” in Solid Phase Peptide Synthesis

Volume: 11 Issue: 4

Author(s): Anna K. Tickler, Andrew B. Clippingdale and John D. Wade

Affiliation:

Keywords: amyloid, solid phase peptide synthesis

Abstract: The phenomenon of “difficult sequence” has long frustrated chemists in their efforts to assemble peptides that contain such sequences by solid phase synthesis methods. A variety of remedial measures are available to minimize or even abolish the negative impact of these sequences during synthesis. These include the use of elevated temperatures and stronger acylating reagents. Amyloid-β, a fragment of the amyloid precursor protein, contains 40-43 residues and possesses a C-terminal sequence that is particularly resistant to ready solid phase synthesis making it a “difficult sequence” peptide. This review focuses on approaches to successfully assemble the peptide by both Boc- and Fmoc solid phase synthesis.

Cite this article as:

Tickler K. Anna, Clippingdale B. Andrew and Wade D. John, Amyloid-β as a “Difficult Sequence” in Solid Phase Peptide Synthesis, Protein & Peptide Letters 2004; 11 (4) . https://dx.doi.org/10.2174/0929866043406986