Synthesis of peptide C-terminal derivatives using the transfer active ester condensation technique

Wang, Pu; Shaw, K. T.; Whigham, B.; Ramage, R.

doi:10.1016/s0040-4039(98)01917-0

Cited by 34 publications

(20 citation statements)

References 17 publications

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“…Some previously reported routes to C-terminal thioesters and active esters via A [17] MeDBZ cyclization and B [18-22] acyl hydrazide oxidation. C This work.…”

Section: Figurementioning

confidence: 99%

“…These methods include, but are not limited to on-resin cyclization of 3,4-diaminobenzoic acid (Dbz) and 3-amino-4-(methylamino)benzoic acid (MeDbz) to their corresponding N-acyl urea (Figure 1A) , [16,17] or solution phase oxidation of Dbz and C-terminal hydrazides to the corresponding benzotriazole and acyl-azide respectively (Figure 1B) . [18–22] While these solution-based methods have been employed in the synthesis of complex proteins, the required oxidants which are typically used in large excess cannot be employed in concert with N-terminal thiazolidines, a common peptide protecting strategy utilized in the synthesis of proteins requiring multiple ligations, aryl amines, or other redox-sensitive residues which can be incorporated via SPPS. Thus, the required activating agents may preclude their use as a general strategy.…”

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confidence: 99%

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Leveraging the Knorr Pyrazole Synthesis for the Facile Generation of Thioester Surrogates for use in Native Chemical Ligation

et al. 2018

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Facile synthesis of C-terminal thioesters is integral to native chemical ligation (NCL) strategies for chemical protein synthesis. We introduce a new method of mild peptide activation, which leverages solid-phase peptide synthesis (SPPS) on an established resin linker and classical heterocyclic chemistry to convert C-terminal peptide hydrazides into their corresponding thioesters via an acyl pyrazole intermediate. Peptide hydrazides, synthesized on established trityl chloride resins, can be activated in solution with stoichiometric acetyl acetone (acac), readily proceed to the peptide acyl pyrazoles. Acyl pyrazoles are mild acylating agents and are efficiently exchanged with an aryl thiol, which can then be directly utilized in NCL. The mild, chemoselective, and stoichiometric activating conditions allow this method to be utilized through multiple sequential ligations without intermediate purification steps.

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“…Some previously reported routes to C-terminal thioesters and active esters via A [17] MeDBZ cyclization and B [18-22] acyl hydrazide oxidation. C This work.…”

Section: Figurementioning

confidence: 99%

mentioning

confidence: 99%

Leveraging the Knorr Pyrazole Synthesis for the Facile Generation of Thioester Surrogates for use in Native Chemical Ligation

et al. 2018

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“…However, unlike Boc-SPPS in situ neutralization protocol [14], Fmoc-SPPS protocol is generally incompatible with the synthesis of peptide-α-thioesters because of inherent base lability of its thioester moiety [15]. To overcome this limitation, several base-stable linkers such as sulfonamide [16][17][18][19], N-acyl-benzimidazolinone [20,21], hydrazide [22,23], cysteine derivatives [24][25][26][27] and thioethylalkylamide derivatives [28][29][30][31][32][33][34] have been developed as thioester precursors. Peptides having these linkers can be prepared by Fmoc-SPPS protocol and converted into corresponding thioesters through trans-thioesterifications.…”

Section: Introductionmentioning

confidence: 99%

An efficient solid‐phase synthesis of peptidyl‐N‐acetylguanidines for use in native chemical ligation

Okamoto

Isoe

Izumi

et al. 2016

Journal of Peptide Science

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In the modern protocols of chemical protein syntheses, peptide-α-thioesters have been used as key components for the assembly of full-length polypeptides through chemoselective peptide coupling reactions. A variety of thioester precursors have been developed for the synthesis of the peptide-α-thioesters by Fmoc solid phase peptide synthesis (Fmoc-SPPS). Recently our group found a peptidyl-N-acetylguanidine as a new peptide-α-thioester precursor. This peptide derivative can be converted into a corresponding peptide-α-thioester only by treatment with an excess amount of a thiol in aqueous buffers at around neutral pH. This unique property allowed us to envision the practical use of the peptidyl-N-acetylguanidines for the chemical syntheses of proteins; however, an efficient synthetic method has been lacking. Herein, we report an efficient solid-phase synthesis of peptidyl-N-acetylguanidines. This new synthetic method employing selective activation and cleavage of a peptide bond successfully provided peptidyl-N-acetylguanidines from the on-resin protected peptides prepared by standard Fmoc-SPPS. We also evaluated the reactivity of a peptidyl-N-acetylguanidine in native chemical ligation through the synthesis of glucose-dependent insulinotropic polypeptide analogue. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.

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“…This thioester bond can be cleaved by the addition of several exogenous thiols to yield polypeptide-αthioester that is useful for semisynthesis of protein under the EPL concept [4][5][6]. In this method, hydrazine can also be used instead of exogenous thiol to obtain polypeptide-α-hydrazide that is stable and can be efficiently converted into polypeptide-α-thioesters under acidic oxidative conditions [7][8][9]. Recently, a unique thioesterification method based on N to S acyl migration was also found [3,10].…”

Section: Introductionmentioning

confidence: 99%

Efficient synthesis of polypeptide‐α‐thioester by the method combining polypeptide expression and chemical activation for the semi‐synthesis of interferon‐γ having oligosaccharides

Kajihara

Kanemitsu

Nishihara

et al. 2014

Journal of Peptide Science

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In order to synthesize interferon-γ glycoform having an oligosaccharide at the 97 position by a semi-synthetic method, interferon-γ-polypeptide-(1-94)-α-hydrazide was prepared by the specific Cys-cyanylation of polypeptide-(1-94)-Cys-His6 expressed from E. coli and subsequent hydrazinolysis in 22% yield (two steps). This polypeptide-α-hydrazide was then converted into corresponding polypeptide-α-thioester under NaNO2 /acid conditions followed by thiolysis in 83% yield.

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Synthesis of peptide C-terminal derivatives using the transfer active ester condensation technique

Cited by 34 publications

References 17 publications

Leveraging the Knorr Pyrazole Synthesis for the Facile Generation of Thioester Surrogates for use in Native Chemical Ligation

Leveraging the Knorr Pyrazole Synthesis for the Facile Generation of Thioester Surrogates for use in Native Chemical Ligation

An efficient solid‐phase synthesis of peptidyl‐N‐acetylguanidines for use in native chemical ligation

Efficient synthesis of polypeptide‐α‐thioester by the method combining polypeptide expression and chemical activation for the semi‐synthesis of interferon‐γ having oligosaccharides

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