Solid-phase peptide synthesis experiences efficiency limits and side reactions when synthesizing peptides exceeding certain lengths.
Solid-phase peptide synthesis faces well-documented limitations in efficiency and encounters side reactions or aggregation as peptide chain length increases, often requiring specialized strategies for longer sequences.
Multiple papers discuss how solid-phase peptide synthesis experiences kinetic drops, aggregation, and efficiency limits when assembling longer or challenging sequences, supporting the claim.
Anna K. Tickler, John D. Wade. Overview of Solid Phase Synthesis of “Difficult Peptide” Sequences. 2007. https://doi.org/10.1002/0471140864.ps1808s50
Discusses how certain longer or 'difficult peptides' resist efficient assembly during solid-phase synthesis due to sequence and length limitations.
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Martin Quibell, Tony Johnson. Difficult peptides. 1999. https://doi.org/10.1093/oso/9780199637256.003.0009
Notes that solid-phase peptide synthesis encounters sudden drops in reaction kinetics and incomplete amino-acylation typically 6-12 residues into the assembly of difficult sequences.
Seraydarian MR, Connolly MD, Zuckermann RN, Kirshenbaum K. Native Chemical Ligation of Peptoid Oligomers.. 2026. https://doi.org/10.1021/acs.biochem.5c00833
Highlights that iterative solid-phase reaction schemes are often limited in their ability to attain protein-like chain lengths, necessitating convergent methods.
Al Musaimi O, Williams DR. OBIMAP (One-Bead Interchain Multipeptide Assembly Platform).. 2026. https://doi.org/10.1021/acsbiomedchemau.5c00237
Notes that traditional solid-phase peptide synthesis faces efficiency hurdles when constructing larger therapeutic peptides ranging from 30 to 60 amino acids.
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