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

Okamoto, Ryo; Isoe, M.; Izumi, Masayuki; Kajihara, Yasuhiro

doi:10.1002/psc.2872

Cited by 7 publications

(3 citation statements)

References 55 publications

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“…In terms of the preparation of peptide thioacids, the current experiments described here used SPPS. Because several groups have reported the preparation of peptide thioacids from peptide thioester and peptide hydrazide, we can use longer peptide thioacids that can be prepared from peptide thioesters by an Intein system , or chemical thioesterification method − with E. coli expression methods. However, dependent on peptide sequence and length, the combination of DDC with NCL and EPL is more practical for the preparation of the N-terminal long peptide of glycoproteins.…”

Section: Discussionmentioning

confidence: 99%

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

et al. 2021

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Glycosylation is a major modification of secreted and cell surface proteins, and the resultant glycans show considerable heterogeneity in their structures. To understand the biological processes arising from each glycoform, the preparation of homogeneous glycoproteins is essential for extensive biological experiments. To establish a more robust and rapid synthetic route for the synthesis of homogeneous glycoproteins, we studied several key reactions based on amino thioacids. We found that diacyl disulfide coupling (DDC) formed with glycosyl asparagine thioacid and peptide thioacid yielded glycopeptides. This efficient coupling reaction enabled us to develop a new glycoprotein synthesis method, such as the bifunctional thioacid-mediated strategy, which can couple two peptides with the N-and C-termini of glycosyl asparagine thioacid. Previous glycoprotein synthesis methods required valuable glycosyl asparagine in the early stage and subsequent multiple glycoprotein synthesis routes, whereas the developed concept can generate glycoproteins within a few steps from peptide and glycosyl asparagine thioacid. Herein, we report the characterization of the DDC of amino thioacids and the efficient ability of glycosyl asparagine thioacid to be used for robust glycoprotein semisynthesis.

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Section: Discussionmentioning

confidence: 99%

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

et al. 2021

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“…Okamoto et al synthesized peptide‐ N ‐acetaminoguanidine Fmoc‐SPPS by solid‐phase method. This method has no obvious reaction to acetaminoguanidine, and the synthesis efficiency of peptide‐ N ‐acetaminoguanidine is high 91 …”

Section: Production Methods Of Bioactive Peptidesmentioning

confidence: 99%

“…This method has no obvious reaction to acetaminoguanidine, and the synthesis efficiency of peptide-N-acetaminoguanidine is high. 91 Yu et al demonstrated a hybrid solid solution-phase connection method that combines the efficiency of solidphase connection and solution-phase connection in the total synthesis of modified histone proteins. The study maximized product yield by performing resin cleavage at the external Rink linker, followed by cleavage at the internal cyclohexamethylenebisacetamide linker to generate natural carboxyl ends.…”

Section: Solid-phase Peptide Synthesismentioning

confidence: 99%

Recent research progress of biologically active peptides

et al. 2022

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With the rapid development of molecular biology and biochemical technology, great progress has been made in the study of peptides. Peptides are easy to digest and absorb, with lowering of blood pressure and cholesterol, improving immunity, regulating hormones, antibacterial, and antiviral effects. Peptides also have physiological regulation and biological metabolism functions with applications in the fields of feed production and biomedical research. In the future, the research focus of bioactive peptides will focus on their efficient preparation and application. This article introduces a comprehensive review of the types, synthesis, functionalization, and bio‐related applications of bioactive peptides. For this aim, we introduced in detail various biopeptides and then presented the production methods of bioactive peptides, such as enzymatic synthesis, microbial fermentation, chemical synthesis, and others. The applications of bioactive peptides for anticancers, immune therapy, antibacterial, and other applications have been introduced and discussed. And discussed the development prospects of biologically active peptides.

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Amide‐Forming Ligation Reactions

2019

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One of the long‐standing pursuits of synthetic organic chemists is the development of chemical methods for the synthesis of peptides and proteins as tools for understanding biological processes and providing therapeutic solutions to human diseases. The advent of chemoselective ligation reactions for the chemical synthesis of peptides and proteins has enabled synthetic chemists to realize this long‐held dream. In an amide‐forming ligation reaction, two uniquely placed functional groups within the peptide allow peptide or protein segments to be joined in a chemoselective manner with an amide bond. In this chapter, some of the early methods based on principles of the capture/rearrangement strategy for ligation of peptides are catalogued, followed by some of the most versatile and well‐established contemporary methods for the preparation of linear/cyclic peptides and proteins such as the native chemical ligation (NCL) and the α‐ketoacid–hydroxylamine (KAHA) ligation. The chapter concludes with some of the most promising new generation ligation methods such as the potassium acyltrifluoroborate–hydroxylamine (KAT) ligation. The tremendous progress in the past two decades in the development of several ligation methods that rely on a pair of unique functional groups is set to expand the horizons of fully functional proteins and multi‐protein assemblies that are purely synthetically prepared. Although contemporary ligation reactions do not match the speed and efficiency at which proteins are assembled in biological systems, the repertoire of chemoselective amide‐forming ligation methods has already enabled synthetic protein chemistry to surpass biology in terms of chemical and structural diversity.

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

Cited by 7 publications

References 55 publications

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

Recent research progress of biologically active peptides

Amide‐Forming Ligation Reactions

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