Rapid Microwave-Assisted Solid-Phase Glycopeptide Synthesis

Matsushita, Takahiko; Hinou, Hiroshi; Kurogochi, Masaki; Shimizu, H.; Nishimura, Shin‐Ichiro

doi:10.1021/ol0474352

Cited by 108 publications

(79 citation statements)

References 20 publications

(11 reference statements)

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“…Reaction mixtures were then digested with 100 g of Pronase (Calbiochem) for the purification by gel filtration chromatography (GFC). N-Glycans were fractionated by GFC using a Bio-Gel P-4 column (200 -400 mesh, Bio-Rad) with H 2 O as the eluant, and the carbohydrate-containing fractions were subjected to 2-aminopyridylation through the reductive amination with a large excess of 2-aminopyridine (Wako Pure Chemical Co. Ltd.) (pH 6.8) in the presence of sodium cyanoborohydride (Sigma) at 90°C for 1 h according to the general protocol (17). The mixture of PA-derivatized N-glycans was fractionated by GFC on a Sephadex G-15 column (Amersham Biosciences) with 10 mM ammonium bicarbonate solution as eluant.…”

Section: Methodsmentioning

confidence: 99%

Unusual N-Glycan Structures in α-Mannosidase II/IIx Double Null Embryos Identified by a Systematic Glycomics Approach Based on Two-dimensional LC Mapping and Matrix-dependent Selective Fragmentation Method in MALDI-TOF/TOF Mass Spectrometry

Hato

Nakagawa

Kurogochi

et al. 2006

Molecular & Cellular Proteomics

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␣-Mannosidase IIx (MX) is an enzyme closely related to ␣-mannosidase II (MII), a key enzyme in N-glycan biosynthesis that catalyzes the first step in conversion of hybridto complex-type N-glycans in Golgi apparatus. Recently we generated MII/MX double knock-out mice and found that double nulls completely lack the complex-type Nglycans (Akama, T. O., Nakagawa, H., Wong, N. K., SuttonSmith, M., Dell, A., Morris, H. R., Nakayama, J., Nishimura, S. N-Glycosylation of proteins is one of the most ubiquitous post-translational modifications in eukaryotes and is thought to play an important role in development, differentiation, tumor metastasis, immunity, intracellular transport, cell adhesion, and aging (1). Insufficiency of human N-glycan biosynthesis leads to diseases such as congenital disorders of glycosylation (2) and hereditary erythroblastic multinuclearity with positive acidifies serum lysis test (3). N-Glycan biosynthesis involves five steps: (i) formation of a dolichol-linked oligosaccharide intermediate in the endoplasmic reticulum (ER), 1 (ii) en bloc transfer of oligosaccharide Glc3Man9GlcNAc2 from dolichol to Asn residue in the consensus sequence of Asn-X-Ser/ Thr on the nascent polypeptide chain by oligosaccharyltransFrom the ‡Laboratory of Advanced Chemical Biology, Graduate

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Section: Methodsmentioning

confidence: 99%

Unusual N-Glycan Structures in α-Mannosidase II/IIx Double Null Embryos Identified by a Systematic Glycomics Approach Based on Two-dimensional LC Mapping and Matrix-dependent Selective Fragmentation Method in MALDI-TOF/TOF Mass Spectrometry

Hato

Nakagawa

Kurogochi

et al. 2006

Molecular & Cellular Proteomics

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“…The advantage of this technique over conventional methods was demonstrated with the synthesis of a 20-residue glycoprotein carrying five trisaccharide chains in 7 h compared to four days with conventional methods. [43] As reported recently, this technique was applied to the synthesis of monosaccharide AFPG analogues that include Pro residues as a polyproline II helix-inducing element. [44] The peptides were prepared in 4-33 % yield, and required limited purification; this suggests that applications to longer oligomers should be possible.…”

Section: Solid-phase Synthesismentioning

confidence: 99%

“…The recent application of microwave irradiation to solid-phase glycopeptide synthesis has addressed most of these limitations. [43] Coupling of glycosidated Fmoc-Thr or Fmoc-Ser with N-terminal amino acids on a resin under microwave irradiation proceeded in 20 min and 98 % yield per coupling. The advantage of this technique over conventional methods was demonstrated with the synthesis of a 20-residue glycoprotein carrying five trisaccharide chains in 7 h compared to four days with conventional methods.…”

Section: Solid-phase Synthesismentioning

confidence: 99%

Design and Synthesis of Antifreeze Glycoproteins and Mimics

Harding

2010

ChemBioChem

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Antifreeze glycoproteins are an important class of biological antifreezes that have potential applications in many areas of medicine, agriculture and industry in which ice crystal growth is damaging. While the synthesis of antifreeze glycoproteins as pure glycoforms has recently been achieved by using ligation and polymerisation strategies, the routine production of large quantities of pure glycoforms remains challenging. A range of C-linked analogues that are readily produced by solid-phase synthesis have delivered novel compounds that are not biological antifreezes, but are potent, non-cytotoxic, ice-recrystallisation inhibitors. Structure-activity studies, the identification of cyclic antifreeze glycoproteins and conformational studies have provided further insight into the requirements for antifreeze activity. These results, coupled with significant advances in approaches to the routine synthesis of different glycoproteins and mimics, present opportunities for the design and synthesis of novel ice-growth-inhibiting and antifreeze compounds.

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“…Moreover, it is generally believed that undesirable side reactions would also be accelerated by microwave heating and that some coupling reagents are heat sensitive. Nevertheless, SPPS with microwave was successfully applied in the synthesis of peptides [56][57][58].…”

Section: Microwave Synthesismentioning

confidence: 99%

Purity profiling of Peptide Drugs

Verbeken¹

2012

JBABM

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The quality of a peptide drug mainly depends on its impurity profile, with the emphasis on the related impurities. These impurities may be biomedically active, alter the desired efficacy or induce unwanted toxicity, an aspect which is termed the "functional quality" of the peptide drug. Therefore, regulatory authorities have set up guidances or have legally established specification limits to assure a consistent purity of these peptide drugs. For the active pharmaceutical ingredients (APIs), the pharmacopoeial monographs are legally binding. Additional information can be found in regional and international guidelines. For the finished pharmaceutical drug products (FDPs) containing peptide active ingredients, only general guidelines are available. The construction of a complete related-impurity profile is very challenging due to the wide availability of different protecting groups, coupling agents and additives that may be used during peptide synthesis. In addition, chemical degradation, occurring during synthesis, formulation or at storage, may occur as well, including not only so-called pure chemical degradation but interaction with excipients as well. This review provides an update of the regulatory and scientific rationales behind the related impurities in peptide drugs.

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Rapid Microwave-Assisted Solid-Phase Glycopeptide Synthesis

Cited by 108 publications

References 20 publications

Unusual N-Glycan Structures in α-Mannosidase II/IIx Double Null Embryos Identified by a Systematic Glycomics Approach Based on Two-dimensional LC Mapping and Matrix-dependent Selective Fragmentation Method in MALDI-TOF/TOF Mass Spectrometry

Unusual N-Glycan Structures in α-Mannosidase II/IIx Double Null Embryos Identified by a Systematic Glycomics Approach Based on Two-dimensional LC Mapping and Matrix-dependent Selective Fragmentation Method in MALDI-TOF/TOF Mass Spectrometry

Design and Synthesis of Antifreeze Glycoproteins and Mimics

Purity profiling of Peptide Drugs

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