A One‐Pot Three‐Segment Ligation Strategy for Protein Chemical Synthesis

Ollivier, Nathalie; Vicogne, Jérôme; Vallin, Aurélie; Drobecq, Hervé; Desmet, Rémi; Mahdi, Ouafâa El; Leclercq, B.; Goormachtigh, Gautier; Fafeur, Véronique; Melnyk, Oleg

doi:10.1002/anie.201105837

Cited by 129 publications

(93 citation statements)

References 40 publications

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“…How these properties can be exploited for designing efficient sequential ligation strategies will be discussed later in Section 3.3. 31 2. Assembly of three segments in the C-to-N direction Examination of the numerous examples of total protein synthesis reported to date reveals that the assembly was usually achieved by sequential NCL of three unprotected peptide segments in the C-to-N direction.…”

Section: Native Peptide Ligation Methodsmentioning

confidence: 99%

Sequential native peptide ligation strategies for total chemical protein synthesis

2012

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Total chemical synthesis of proteins is usually achieved by assembling unprotected peptide segments using site-specific and chemoselective native peptide ligation methods. Access to large proteins often requires the assembly of at least three segments due to the current limits of solid phase synthesis of individual peptide segments. The aim of this tutorial review is to present the basic concepts and challenges underlying the design of sequential peptide ligation strategies using solution or solid phase chemistry. A special emphasis is given to C-to-N and N-to-C three-segment assembly strategies, which potentially give access to proteins composed of up to 150 amino acid residues.

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Section: Native Peptide Ligation Methodsmentioning

confidence: 99%

Sequential native peptide ligation strategies for total chemical protein synthesis

2012

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“…Other major tools are chemoselective peptide bond forming reactions which enable the coupling of unprotected peptide segments in water. 13,[16][17][18][19][20] While recent advances have led to the development of efficient one-pot three-segment sequential assembly methods, 12,15,[21][22][23] the ligation of more than three segments usually involves time-consuming intermediate isolation or purication steps, accompanied by signicant material losses. 9 The ligation of two peptide segments potentially gives access to polypeptides composed of up to 100 amino acid residues, considering the current limits of SPPS.…”

Section: Introductionmentioning

confidence: 99%

Highly efficient solid phase synthesis of large polypeptides by iterative ligations of bis(2-sulfanylethyl)amido (SEA) peptide segments

et al. 2013

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International audienceUp to now, the advantages of solid phase protein synthesis have been largely under-utilized due to the difficulty of designing a simple and efficient elongation cycle enabling the concatenation of unprotected peptide segments. The combination of selective N-terminal anchoring (N3-Esoc linker) with the blocked thioester properties of SEAoff group enabled the solid phase concatenation of unprotected peptide segments by N-to-C sequential formation of native peptide bonds. The strategy was applied to the synthesis of a 60 amino acid-long latent peptide thioester or to the assembly of five peptide segments to give a 15 kDa polypeptide

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“…[10] Crambin with a V15A mutation has been frequently used as a standard to test new methods for chemical protein synthesis. [3, 4b, 11] Our synthetic strategy is shown in Figure 2 A, where [V15A]-crambin was divided into four peptide segments (10,8,5''', and 6). All the peptide thioesters are prepared through activation and thiolysis of the corresponding peptide hydrazides.…”

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An Efficient One‐Pot Four‐Segment Condensation Method for Protein Chemical Synthesis

et al. 2015

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Successive peptide ligation using a one-pot method can improve the efficiency of protein chemical synthesis. Although one-pot three-segment ligation has enjoyed widespread application, a robust method for one-pot four-segment ligation had to date remained undeveloped. Herein we report a new one-pot multisegment peptide ligation method that can be used to condense up to four segments with operational simplicity and high efficiency. Its practicality is demonstrated by the one-pot four-segment synthesis of a plant protein, crambin, and a human chemokine, hCCL21.

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A One‐Pot Three‐Segment Ligation Strategy for Protein Chemical Synthesis

Cited by 129 publications

References 40 publications

Sequential native peptide ligation strategies for total chemical protein synthesis

Sequential native peptide ligation strategies for total chemical protein synthesis

Highly efficient solid phase synthesis of large polypeptides by iterative ligations of bis(2-sulfanylethyl)amido (SEA) peptide segments

An Efficient One‐Pot Four‐Segment Condensation Method for Protein Chemical Synthesis

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