Protection of carboxamide functions by the trityl residue. Application to peptide synthesis

Sieber, Peter; Riniker, B.

doi:10.1016/s0040-4039(00)74872-6

Cited by 91 publications

(70 citation statements)

References 8 publications

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“…281,279,280 Currently, the most used protecting groups are Xan (9-xanthenyl) and Trt, which are compatible with both Boc/Bn and Fmoc/ t Bu strategies. In the case of the former, the Xan group protects Asn and Gln side chains only during the coupling and is removed during TFA treatments for Boc removal.…”

Section: Generalmentioning

confidence: 99%

“…However, it is not currently widely used because it can cause alkylation of Trp and is reported to give worse results than the Trt group. 290,281 Create PDF files without this message by purchasing novaPDF printer (http://www.novapdf.com) Figure 17. Acylation of the side chain of Arg during amino acid coupling, followed by base-catalyzed deguanidination.…”

Section: Protecting Groups Removed By Acid-9-xanthenyl (Xan)mentioning

confidence: 99%

“…281,282 In the case of 9-xanthenyl, the direct protection of the Fmoc-Asn and Fmoc-Gln has also been described. 283 282 It is removed by 90% TFA and scavengers.…”

Section: Introduction Of the Protecting Groupsmentioning

confidence: 99%

“…283 -Trityl (Trt). 280,281 It is removed with TFA-H 2 O-EDT (90:5:5), and used in both the Boc/Bn and Fmoc/ t Bu strategies. The time required for removal increases from 10 min to more than 4 h when the α-amino of Asn is free.…”

Section: Introduction Of the Protecting Groupsmentioning

confidence: 99%

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Amino Acid-Protecting Groups

2009

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Section: Generalmentioning

confidence: 99%

Section: Protecting Groups Removed By Acid-9-xanthenyl (Xan)mentioning

confidence: 99%

“…281,282 In the case of 9-xanthenyl, the direct protection of the Fmoc-Asn and Fmoc-Gln has also been described. 283 282 It is removed by 90% TFA and scavengers.…”

Section: Introduction Of the Protecting Groupsmentioning

confidence: 99%

Section: Introduction Of the Protecting Groupsmentioning

confidence: 99%

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Amino Acid-Protecting Groups

2009

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“…Coupling difficulties did increase, however, as the length of the peptide increased, although, due to repeated capping, the stoichiometry of the activated species increased with respect to the remaining available amino groups. A possible cause of the problem could be the formation of secondary structures in the peptide on the resin promoted by the use of organic solvents and the concomitant inaccessibility of the active species to the reactive amino functions of the peptidyl-resin [53]. This phenomenon could be important in the case of the B1-domain, which by itself exhibits particularly stable secondary structure elements.…”

Section: E T V T F T K T a D D Y T W E G D V C N D N~y~k F V K E A T~mentioning

confidence: 99%

Synthesis, Three-Dimensional Structure, and Specific 15N-Labelling of the Streptococcal Protein G B1-Domain

et al. 1995

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The 55-amino-acid B1-domain of the streptococcal protein G shows a high binding affinity to IgG isolated from a wide range of mammalian species. Since the B1-domain forms an extremely stable globular folding unit containing the major secondary structure elements and is devoid of proline residues and disulfide bridges, it is also a useful tool for protein folding and stability studies. Its small size makes this protein an ideal candidate for production by chemical synthesis, allowing incorporation of non-natural amino acids with the possibility of assessing the influence of such residues on both the functional and structural characteristics of proteins.In this study, we enployed three successive chemical syntheses of the B1-domain in order to define the optimal conditions of coupling and protection. The stepwise solid-phase methodology using the tertbutyloxycarbonyl/benzyl strategy was used for this purpose.First, the sequence assembly difficulties were evaluated. After analyzing of the problems found during assembly, a second optimized synthesis was performed leading to formation of a synthetic B1-domain with a higher yield; the synthetic B1-domain was completely functional in its binding properties to IgG. Three orthogonal purification steps (gel-permeation, reverse-phase and ion-exchange HPLC) were required to obtain a sample suitable for structural analysis by high-resolution NMR. This study led to the conclusion that the synthetic B 1 -domain adopts a three-dimensional structure identical to that of the molecule obtained by recombinant techniques [Gronenborn, A.

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Synthesis and CD studies of an 88-residue peptide containing the main receptor binding site of HTLV-I SU-glycoprotein

Goetz¹,

Geoffre²,

Busetta³

et al. 1997

J. Peptide Sci.

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Essential HTLV-1 biological functions, like host-cell receptor recognition, depend on the structural motives on the surface glycoprotein gp46. We defined a peptide of 88 amino acids [Arg147-Leu234] corresponding to the central part of the protein sequence, where major neutralizing epitopes are localized. After evaluating the feasibility of its chemical synthesis, the chosen sequence was realized using the stepwise solid-phase methodology. Multiple chromatographic purification steps were required to obtain a sample suitable for structural analysis. Correct folding was supported by strong binding of monooclonal antibodies, recognizing known exposed immunodominant regions. Circular dichroism studies confirmed a non-random conformation of at least 70-80% of the synthetic peptide. Investigation of the 3D-structure of the synthetic peptide will provide useful information for future vaccine and drug-design strategies.

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Protection of carboxamide functions by the trityl residue. Application to peptide synthesis

Cited by 91 publications

References 8 publications

Amino Acid-Protecting Groups

Amino Acid-Protecting Groups

Synthesis, Three-Dimensional Structure, and Specific 15N-Labelling of the Streptococcal Protein G B1-Domain

Synthesis and CD studies of an 88-residue peptide containing the main receptor binding site of HTLV-I SU-glycoprotein

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