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.
Keywords: amyloid, solid phase peptide synthesis
Protein & Peptide Letters
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.
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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
DOI https://dx.doi.org/10.2174/0929866043406986 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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