2017
DOI: 10.1007/s12209-017-0068-8
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Progress in Chemical Synthesis of Peptides and Proteins

Abstract: For the proteins that cannot be expressed exactly by cell expression technology (e.g., proteins with multiple posttranslational modifications or toxic proteins), chemical synthesis is an important substitute. Given the limited peptide length offered by solid-phase peptide synthesis invented by Professor Merrifield, peptide ligation plays a key role in long peptide or protein synthesis by ligating two small peptides to a long one. Moreover, high-molecularweight proteins must be synthesized using two or more pep… Show more

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Cited by 29 publications
(17 citation statements)
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References 107 publications
(104 reference statements)
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“…Considering the often low amounts of AMPs obtained by purification from natural sources and the high costs and difficulties that may arise from chemical synthesis (Li et al, 2010;Hou et al, 2017), recombinant production of AMPs provides a solid option to make these peptides accessible at low cost and high efficiency.…”
Section: Recombinant Production Of Afpsmentioning
confidence: 99%
“…Considering the often low amounts of AMPs obtained by purification from natural sources and the high costs and difficulties that may arise from chemical synthesis (Li et al, 2010;Hou et al, 2017), recombinant production of AMPs provides a solid option to make these peptides accessible at low cost and high efficiency.…”
Section: Recombinant Production Of Afpsmentioning
confidence: 99%
“…Furthermore, compounds 4e, 4h, and 4j containing commonly used side chain protecting groups in Fmoc solid phase peptide synthesis (SPPS) are versatile substrates for peptide elongation and diversification. 18 Importantly, we did not observe any epimerization from the amino acid stereocenter, as indicated by the retained dr from starting materials to products, although in some cases part of the minor diastereomers were lost during the purification process (see Supporting Information).…”
Section: Resultsmentioning
confidence: 72%
“…For a better understanding of protein interactions, structural properties, and ligand binding, the production of soluble and functional recombinant proteins is crucial. While, for small proteins or peptides, both chemical synthesis and E. coli expression systems provide a unique set of advantages and disadvantages [27][28][29][30][31][32][33], we decided on a bacterial expression system for the following reasons: The transfer of the designed constructs into biological systems is easier and the data more comparable. Additionally, applications requiring a coating of the proteins, i.e., ELISA, need larger tags so that binding sites and epitopes are not hidden by the coating process.…”
Section: Discussionmentioning
confidence: 99%