Bis(2-sulfanylethyl)amino Native Peptide Ligation

Ollivier, Nathalie; Dheur, Julien; Mhidia, Reda; Blanpain, Annick; Melnyk, Oleg

doi:10.1021/ol102273u

Cited by 195 publications

(189 citation statements)

References 44 publications

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“…S acyl shift-based method for the synthesis of peptide thioesters [122][123][124][125][126][127][128] which utilizes a C-terminal bis(2-sulfanylethyl)amide (SEA) group. As depicted in Fig.…”

Section: New Methods For Activated Peptide Synthesismentioning

confidence: 99%

“…For example, at slightly elevated temperature, peptides H-ILKEPVHGX-SEA (X¼G, A, Y, or V) 78 were successfully ligated with peptide H-CILKEPVHGV-NH 2 82 to afford peptides H-ILKEPVHGX-CILKEPVHGV-NH 2 83-86 in 32-77% yield (Fig. 10) [122].…”

Section: New Methods For Activated Peptide Synthesismentioning

confidence: 99%

“…The SEA system mentioned previously can also be used in the one-pot, N-to-C direction assembly of three peptide fragments [122]. In 2012, Melnyk and …”

Section: N-to-c Directionmentioning

confidence: 99%

See 2 more Smart Citations

New Methods for Chemical Protein Synthesis

Guan

Chaffey

Zeng

2014

Topics in Current Chemistry

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Chemical protein synthesis is a useful tool to generate pure proteins which are otherwise difficult to obtain in sufficient amounts for structure and property analysis. Additionally, because of the precise and flexible nature of chemical synthesis, it allows for controllable variation of protein sequences, which is valuable for understanding the relationships between protein structure and function. Despite the usefulness of chemical protein synthesis, it has not been widely adopted as a tool for protein characterization, mainly because of the lack of general and efficient methods for the preparation and coupling of peptide fragments and for the folding of polypeptide chains. To address these issues, many new methods have recently been developed in the areas of solid-phase peptide synthesis, peptide fragment assembly, and protein folding. Here we review these recent technological advances and highlight the gaps needing to be addressed in future research.

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Section: New Methods For Activated Peptide Synthesismentioning

confidence: 99%

Section: New Methods For Activated Peptide Synthesismentioning

confidence: 99%

See 1 more Smart Citation

New Methods for Chemical Protein Synthesis

Guan

Chaffey

Zeng

2014

Topics in Current Chemistry

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“…Recently, Dr. Liu group [73] and Dr. Melnyk group [74] showed that a C-terminal BMEA (N,N-bis(2-mercaptoethyl)-amide) peptide can undergo facile intramolecular thiolysis (or N-to-S acyl transfer) to form a thioester (Fig. 21).…”

Section: Nclmentioning

confidence: 99%

Progress in Chemical Synthesis of Peptides and Proteins

Hou

Zhang

Liu

2017

Trans. Tianjin Univ.

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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 peptide ligation steps, and sequential peptide ligation is such an efficient way. In this paper, we reviewed the development of chemical protein synthesis, including solid-phase peptide synthesis, chemical ligation, and sequential chemical ligation.

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“…Several strategies have been employed to overcome this incompatibility: (i) use of the non-nucleophilic bicyclic base 1,8-diazabicyclo[5.4.0]undec-7-ene (DBU) instead of piperidine during the Fmoc removal (Clippingdale et al, 2000); (ii) masking of the thioester group by introducing a stable group at the C-terminus which after completion of the whole sequence is converted into a thioester (Brask et al, 2003); and (iii) the use of alternative resin linkers that produce thioesters during acidic work-up after cleavage from the resin (Ingenito et al, 1999). The recent advances in masking strategies (Liu and Mayer, 2013;Zheng et al, 2013) and the use of dedicated resin-linkers (Hou et al, 2010;Ollivier et al, 2010Ollivier et al, , 2014Hemu et al, 2013;Taichi et al, 2013) have made peptides with a C-terminal thioester group readily accessible for Fmoc-chemistry.…”

Section: Chemical Cyclization Of Peptidesmentioning

confidence: 99%

Sortase-mediated backbone cyclization of proteins and peptides

Hof

Maňásková²,

Veerman

et al. 2015

Biological Chemistry

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Backbone cyclization has a profound impact on the biological activity and thermal and proteolytic stability of proteins and peptides. Chemical methods for cyclization are not always feasible, especially for large peptides or proteins. Recombinant Staphylococcus aureus sortase A shows potential as a new tool for the cyclization of both proteins and peptides. In this review, the scope and background of the sortase-mediated cyclization are discussed. High efficiency, versatility, and easy access make sortase A a promising cyclization tool, both for recombinant and chemo-enzymatic production methods.

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Bis(2-sulfanylethyl)amino Native Peptide Ligation

Cited by 195 publications

References 44 publications

New Methods for Chemical Protein Synthesis

New Methods for Chemical Protein Synthesis

Progress in Chemical Synthesis of Peptides and Proteins

Sortase-mediated backbone cyclization of proteins and peptides

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