Novel version of Multiple Antigenic Peptide allowing incorporation on a cysteine functionalized lysine tree

Baleux, Françoise; Dubois, Philippe

doi:10.1111/j.1399-3011.1992.tb00098.x

Cited by 16 publications

(6 citation statements)

References 18 publications

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“…The high molecular weight of peptide 8 complicated its NMR analysis. A detailed 1 H, 13 C, COSY, TOSCY, HSQC and HMBC NMR study of the bond formed during the ligation process was performed using peptide 13 H-C(CO-IKA-NH 2 )YG-NH 2 (71% yield), obtained by ligating cysteinyl tripeptide 11 H-CYG-NH 2 with phenylthiocarbamate 12 PhSCO-IKA-NH 2 (see Supporting information). The CO-NH proton of Ile residue appeared as a doublet at 8.65 ppm (DMF-d 7 ).…”

Section: Resultsmentioning

confidence: 99%

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Thiocarbamate‐linked peptides by chemoselective peptide ligation

Besret

Ollivier

Blanpain

et al. 2008

Journal of Peptide Science

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Peptide chemical ligation chemistries, which allow the chemoselective coupling of unprotected peptide fragments, are useful tools for synthesizing native polypeptides or unnatural peptide-based macromolecules. We show here that the phenylthiocarbonyl group can be easily introduced into peptides on alpha or epsilon amino groups using phenylthiochloroformate and standard solid-phase method. It reacts chemoselectively with cysteinyl peptides to give an alkylthiocarbamate bond. S,N-shift of the alkylaminocarbonyl group from the Cys side chain to the alpha-amino group did not occur. The method was used for linking two peptide chains through their N-termini, for the synthesis of a cyclic peptide or for the synthesis of di- or tetravalent multiple antigenic peptides (MAPs). Thiocarbamate ligation is thus complementary to thioether, thioester or disulfide ligation methods.

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Section: Resultsmentioning

confidence: 99%

“…Other methods result in the formation of unnatural covalent bonds such as disulfide [13], oxime [14], hydrazone [15][16][17][18], thioether [13], thiazolidine [18,19], thioester [20] and 1,2,3-triazole linkages [21]. These methods are of great interest when native peptide bonds are not absolutely required.…”

Section: Introductionmentioning

confidence: 99%

Thiocarbamate‐linked peptides by chemoselective peptide ligation

Besret

Ollivier

Blanpain

et al. 2008

Journal of Peptide Science

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“…The membrane support used for arrays is usually cellulose, which is compatible with Fmoc-based peptide synthesis and the biological assay [ 1 , 15 ]. For other chemistries non-compatible with nitrocellulose, alternative material may be used, such as polytetrafluoroethylene (PTFE) membranes or polyethylene films [ 16 , 17 , 18 ], glass [ 19 ] or metal films. The choice of the support conditions the immobilization strategies, peptide density and detection method to analyze the array.…”

Section: Introductionmentioning

confidence: 99%

Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment

2021

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PEPscan is an old approach that has recently gained renewed interest for the identification of interfering peptides (IPs), i.e., peptides able to interfere with protein–protein interactions (PPIs). Its principle is to slice a protein sequence as a series of short overlapping peptides that are synthesized on a peptide array and tested for their ability to bind a partner, with positive spots corresponding to candidate IPs. PEPscan has been applied with a rather large success in various contexts, but the structural determinants underlying this success remain obscure. Here, we analyze the results of 14 PEPscan experiments, and confront the in vitro results with the available structural information. PEPscan identifies candidate IPs in limited numbers that in all cases correspond to solvent-accessible regions of the structures, their location at the protein–protein interface remaining to be further demonstrated. A strong point of PEPscan seems to be its ability to identify specific IPs. IPs identified from the same protein differ depending on the target PPI, and correspond to patches not frequently involved in the interactions seen in the 3D structures available. Overall, PEPscan seems to provide a cheap and rapid manner to identify candidate IPs, that also comes with room for improvement.

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“…1B), by derivatising the Lys dendron core with thiol groups and reacting it with XAcfunctionalised peptide epitopes. While conjugation of thiol-functionalised Lys-based dendrons with peptide epitopes via disulfide bonds has been described, 9,21 it has not enjoyed wide acceptance, possibly because the complexity of thiol-disulfide exchange reactions made the approach difficult to control. We have revisited the strategy with a substantial improvement, namely replacing disulfide-by thioether-based ligation, which to the best of our knowledge has not been attempted before in the reverse format proposed here, either in solution or in the solid phase.…”

Section: Introductionmentioning

confidence: 99%

Reverse thioether ligation route to multimeric peptide antigens

et al. 2012

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Multimeric presentation, a rather effective way of enhancing peptide immunogenicity, is best exemplified by MAP (multiple antigenic peptide) dendrimers consisting of a branched Lys core on which several copies of the peptide epitope are displayed. While accessible by solid-phase synthesis, MAPs can also be conveniently made in solution, e.g., by linking the epitope (N-acetylated and with a C-terminal Cys) through a thioether bond onto the α and ε (haloacetyl-activated) positions of the Lys core. We now report the reverse version of this approach, whereby a chloroacetyl-derivatised epitope is tethered to a thiol-functionalised form of a Lys dendron core. This convergent approach can be carried out either in solution or in the solid phase and is advantageous because (i) in situ tris(2-carboxyethyl)phosphine (TCEP)-mediated reduction of disulfide bonds maintains the thiol platform reactive throughout the ligation process; (ii) the low amounts of TCEP used pose minimal risk to chloroacetyl groups in the peptide, resulting in (iii) significantly reduced byproduct formation, hence cleaner products. For the solid phase version of the method, an optimised procedure has been devised to convert the Lys core into a tetrathiol dendron.

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Novel version of Multiple Antigenic Peptide allowing incorporation on a cysteine functionalized lysine tree

Cited by 16 publications

References 18 publications

Thiocarbamate‐linked peptides by chemoselective peptide ligation

Thiocarbamate‐linked peptides by chemoselective peptide ligation

Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment

Reverse thioether ligation route to multimeric peptide antigens

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