Evaluation of new base‐labile2‐(4‐nitrophenylsulfonyl)ethoxycarbonyl (Nsc)‐amino acids for solid‐phase peptide synthesis

Balse, Preeti; Han, Guoxia; Hruby, Victor J.; Kim, H.J.

doi:10.1034/j.1399-3011.2000.00759.x

Cited by 10 publications

(8 citation statements)

References 20 publications

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“…In conclusion, the Nsc group can be considered an alternative to Fmoc for N α ‐protection 34, 36, 46. Nsc‐amino acids are more suitable for use in automatic synthesizers where amino acid derivatives are stored in solution over relatively long periods or when protected peptides are left to react in a convergent strategy.…”

Section: Nα‐amino Protecting Groupsmentioning

confidence: 99%

Orthogonal protecting groups forNα-amino andC-terminal carboxyl functions in solid-phase peptide synthesis

Alberício¹

2000

Biopolymers

105

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For the controlled synthesis of even the simplest dipeptide, the Nα‐amino group of one of the amino acids and the C‐terminal carboxyl group of the other should both be blocked with suitable protecting groups. Formation of the desired amide bond can now occur upon activation of the free carboxyl group. After coupling, peptide synthesis can be continued by removal of either of the two protecting groups and coupling with the free C‐terminus or Nα‐amino group of another protected amino acid. When three functional amino acids are present in the sequence, the side chain of these residues also has to be protected. It is important that there is a high degree of compatibility between the different types of protecting groups such that one type may be removed selectively in the presence of the others. At the end of the synthesis, the protecting groups must be removed to give the desired peptide. Thus, it is clear that the protection scheme adopted is of the utmost importance and makes the difference between success and failure in a given synthesis. Since R. B. Merrifield introduced the solid‐phase strategy for the synthesis of peptides, this prerequisite has been readily accepted. This strategy is usually carried out using two main protection schemes: the tert‐butoxycarbonyl/benzyl and the 9‐flourenylmethoxycarbonyl/tert‐butyl methods. However, for the solid‐phase preparation of complex or fragile peptides, as well as for the construction of libraries of peptides or small molecules using a combinatorial approach, a range of other protecting groups is also needed. This review summarizes other protecting groups for both the Nα‐amino and C‐terminal carboxyl functions. © 2000 John Wiley & Sons, Inc. Biopoly 55: 123–139, 2000

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Section: Nα‐amino Protecting Groupsmentioning

confidence: 99%

Orthogonal protecting groups forNα-amino andC-terminal carboxyl functions in solid-phase peptide synthesis

Alberício¹

2000

Biopolymers

105

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“…[19] Unfortunately, it was subsequently shown to produce less pure peptides to those prepared using Fmoc protection. [20] The 2,2-[bis(4-nitrophenyl)]ethoxycarbonyl (Bnpeoc) group is also more base-labile than the Fmoc group. [21] However, none of the many reported base-labile protecting groups have supplanted Fmoc in terms of ease of preparation, cost-effectiveness, and subsequent use in chemical synthesis strategies, including SPPS.…”

Section: N a -Fmoc Groupmentioning

confidence: 99%

The 9-Fluorenylmethoxycarbonyl (Fmoc) Group in Chemical Peptide Synthesis – Its Past, Present, and Future

Li¹,

O'Brien-Simpson²,

Hossain³

et al. 2020

Aust. J. Chem.

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The chemical formation of the peptide bond has long fascinated and challenged organic chemists. It requires not only the activation of the carboxyl group of an amino acid but also the protection of the N a -amino group. The more than a century of continuous development of ever-improved protecting group chemistry has been married to dramatic advances in the chemical synthesis of peptides that, itself, was substantially enhanced by the development of solid-phase peptide synthesis by R. B. Merrifield in the 1960s. While the latter technology has continued to undergo further refinement and improvement in both its chemistry and automation, the development of the base-labile 9-fluorenylmethoxycarbonyl (Fmoc) group and its integration into current synthesis methods is considered a major landmark in the history of the chemical synthesis of peptides. The many beneficial attributes of the Fmoc group, which have yet to be surpassed by any other N a -protecting group, allow very rapid and highly efficient synthesis of peptides, including ones of significant size and complexity, making it an even more valuable resource for research in the post-genomic world. This review charts the development and use of this N a -protecting group and its adaptation to address the need for more green chemical peptide synthesis processes.

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“…New base-labile N a -protecting groups The 2-(4-nitrophenylsulfonyl)ethoxycarbonyl group Nsc (see Table 4.1) has recently been considered as a valuable alternative to the Fmoc group, because it is more base-stable and, therefore, less sensitive towards weakly basic media [53][54][55]. Nsc is more hydrophilic than Fmoc, and less prone to aspartimide formation.…”

Section: Alkoxycarbonyl-type (Urethane-type) Protecting Groupsmentioning

confidence: 99%

Peptide Synthesis

Sewald

Jakubke

2009

Peptides: Chemistry and Biology

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Evaluation of new base‐labile2‐(4‐nitrophenylsulfonyl)ethoxycarbonyl (Nsc)‐amino acids for solid‐phase peptide synthesis

Cited by 10 publications

References 20 publications

Orthogonal protecting groups forNα-amino andC-terminal carboxyl functions in solid-phase peptide synthesis

Orthogonal protecting groups forNα-amino andC-terminal carboxyl functions in solid-phase peptide synthesis

The 9-Fluorenylmethoxycarbonyl (Fmoc) Group in Chemical Peptide Synthesis – Its Past, Present, and Future

Peptide Synthesis

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