SOLID‐PHASE PEPTIDE SYNTHESIS USING MILD BASE CLEAVAGE OF <i>N</i><sub>α</sub>FLUORENYLMETHYLOXYCARBONYLAMINO ACIDS, EXEMPLIFIED BY A SYNTHESIS OF DIHYDROSOMATOSTATIN

Chang, Chi‐Deu; Meienhofer, Johannes

doi:10.1111/j.1399-3011.1978.tb02845.x

Cited by 291 publications

(72 citation statements)

References 28 publications

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“…This method also makes it feasible to use a large excess of reagents to drive the reaction to completion and carry out multi-step syntheses with relatively high yields. Solid phase synthesis techniques have been successfully used to make peptides (43)(44)(45), including mycobactins (46).…”

Section: Isolation Of Individual Molecularmentioning

confidence: 99%

Synthesis of Dideoxymycobactin Antigens Presented by CD1a Reveals T Cell Fine Specificity for Natural Lipopeptide Structures

Young

Kasmar

Moraski

et al. 2009

Journal of Biological Chemistry

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Mycobacterium tuberculosis survival in cells requires mycobactin siderophores. Recently, the search for lipid antigens presented by the CD1a antigen-presenting protein led to the discovery of a mycobactin-like compound, dideoxymycobactin (DDM). Here we synthesize DDMs using solution phase and solid phase peptide synthesis chemistry. Comparison of synthetic standards to natural mycobacterial mycobactins by nuclear magnetic resonance and mass spectrometry allowed identification of an unexpected ␣-methyl serine unit in natural DDM. This finding further distinguishes these pre-siderophores as foreign compounds distinct from conventional peptides, and we provide evidence that this chemical variation influences the T cell response. One synthetic DDM recapitulated natural structures and potently stimulated T cells, making it suitable for patient studies of CD1a in infectious disease. DDM analogs differing in the stereochemistry of their butyrate or oxazoline moieties were not recognized by human T cells. Therefore, we conclude that T cells show precise specificity for both arms of the peptide, which are predicted to lie at the CD1a-T cell receptor interface.

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Section: Isolation Of Individual Molecularmentioning

confidence: 99%

Synthesis of Dideoxymycobactin Antigens Presented by CD1a Reveals T Cell Fine Specificity for Natural Lipopeptide Structures

Young

Kasmar

Moraski

et al. 2009

Journal of Biological Chemistry

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“…The lyophilized samples were dissolved in dimethyl sulfoxide-d 6 (DMSO-d 6 ) at a concentration of 10 mg/mL. One hundred and twenty-eight scans were recorded during each 1 H-NMR measurement.…”

Section: H-nmrmentioning

confidence: 99%

“…To synthesize peptides, solid phase peptide synthesis requiring protection-deprotection procedures is generally used [4][5][6]. Peptides can also be biosynthesized by using recombinant DNA expression systems, in which amino acid sequences influence protein yield as well as productivity, and multistep purifications are necessary [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit

Yazawa

Numata

2016

Polymers

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Abstract:Peptides have the potential to serve as an alternative for petroleum-based polymers to support a sustainable society. However, they lack thermoplasticity, owing to their strong intermolecular interactions. In contrast, nylon is famous for its thermoplasticity and chemical resistance. Here, we synthesized peptides containing a nylon unit to modify their thermal properties by using papain-catalyzed chemoenzymatic polymerization. We used L-glutamic acid alkyl ester as the amino acid monomer and nylon 1, 3, 4, and 6 alkyl esters as the nylon unit. Papain catalyzed the copolymerization of glutamic acid with nylon 3, 4, and 6 alkyl esters, whereas the nylon 1 unit could not be copolymerized. Other proteases used in this study, namely, bromelain, proteinase K, and Candida antarctica lipase (CALB), were not able to copolymerize with any nylon units. The broad substrate specificity of papain enabled the copolymerization of L-glutamic acid with a nylon unit. The peptides with nylon units demonstrated different thermal profiles from that of oligo(L-glutamic acid). Therefore, the resultant peptides with various nylon units are expected to form fewer intermolecular hydrogen bonds, thus altering their thermal properties. This finding is expected to broaden the applications of peptide materials and chemoenzymatic polymerization.

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“…O- Peptide Synthesis Fragment peptides corresponding to amino acid sequence from human prion protein were synthesized using an automated ABI model 433A peptide synthesizer (0.1 mmol scale with preloaded resin) from Fmoc protected L-amino acid derivatives purchased from ABI. 44,45) Amino acids were preactivated by reaction with HATU and DIEA. After deprotection according to the manufacturer's protocol, each peptide was purified using reversed-phase HPLC (Capcell Pak C18 column, SG, 10 or 15 mm i.d.ϫ250 mm; Shiseido Co., Ltd., Japan) with a linear gradient elution from 0.1% TFA to 50% or 70% CH 3 CN containing 0.1% TFA over 30 min.…”

mentioning

confidence: 99%

Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

Kojima

Konishi

et al. 2011

CHEMICAL & PHARMACEUTICAL BULLETIN

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Regular ArticlePrion protein (PrP) is a cell-surface glycoprotein implicated in the pathogenesis of a range of neurodegenerative disorders collectively termed transmissible spongiform encephalopathies (TSEs), including Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (BSE) in cows, and chronic wasting disease (CWD) in deer.1-4) PrP exists in two distinct forms: cellular PrP (PrP C ) and a pathogenic or scrapie form (PrP Sc ) derived from PrP C . Although there is no difference in the primary structure of these isoforms, spectroscopic studies revealed that PrP C has a high ahelical content, whereas PrP Sc is composed primarily of bsheets. 5,6) There are many hypotheses regarding the conversion of PrP C to PrP Sc , but the data suggest that conversion is entirely conformational and involves no amino acid substitutions or deletions, and thus supports the protein-only hypothesis.2) Prion replication requires the conversion of PrP C into PrP Sc , where PrP Sc acts as a template and protein X functions as a chaperone. [7][8][9] Mature human PrP (hPrP) consists of 253 amino acids, with a C-terminal glycosylphosphatidylinositol (GPI) anchor and two glycosylation sites (Fig. 1). The N-terminal domain, which includes four repeats of the PHGGGWGQ octapeptide, is a flexibly disordered region. In contrast, the C-terminal domain, which includes two a-helices and a GPI anchor, is a folded region. The middle domain includes two b-sheets and one a-helix.10-12) The hPrP region spanning amino acid residues 106-126 in the middle domain is thought to be responsible for the pathogenic properties of PrP Sc , including neurotoxicity, protease-resistance, induction of hypertrophy, and promotion of astrocyte proliferation. [13][14][15][16][17] Although PrP metal-binding sites have been investigated using full-length PrP C or synthetic fragment peptides and it is now generally accepted that PrP C binds copper in vivo, 18) most researchers have focused on the octarepeat region, [19][20][21][22][23] and there are few reports describing the metal-binding ability of the middle-and C-terminal domains of hPrP.24) The interaction of full-length and truncated forms of PrP with Cu 2+ has been investigated using a range of techniques, including electron paramagnetic resonance (EPR), [25][26][27] We developed a column switch (CS)-HPLC system that can detect direct metal-binding to the octarepeat region of hPrP C , and the data obtained using our CS-HPLC method agreed well with previous CD analyses. 42,43) In this study, we used CS-HPLC to analyze the metal-binding characteristics of 21 synthetic fragment peptides derived from the sequence of hPrP amino acids 60-230. Key words prion protein; metal-binding; metal chelate affinity column; column switch HPLC; synthetic peptide Chem. Pharm. Bull. 59(8) 965-971 (2011)

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SOLID‐PHASE PEPTIDE SYNTHESIS USING MILD BASE CLEAVAGE OF N_αFLUORENYLMETHYLOXYCARBONYLAMINO ACIDS, EXEMPLIFIED BY A SYNTHESIS OF DIHYDROSOMATOSTATIN

Cited by 291 publications

References 28 publications

Synthesis of Dideoxymycobactin Antigens Presented by CD1a Reveals T Cell Fine Specificity for Natural Lipopeptide Structures

Synthesis of Dideoxymycobactin Antigens Presented by CD1a Reveals T Cell Fine Specificity for Natural Lipopeptide Structures

Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit

Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

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SOLID‐PHASE PEPTIDE SYNTHESIS USING MILD BASE CLEAVAGE OF NαFLUORENYLMETHYLOXYCARBONYLAMINO ACIDS, EXEMPLIFIED BY A SYNTHESIS OF DIHYDROSOMATOSTATIN

Cited by 291 publications

References 28 publications

Synthesis of Dideoxymycobactin Antigens Presented by CD1a Reveals T Cell Fine Specificity for Natural Lipopeptide Structures

Synthesis of Dideoxymycobactin Antigens Presented by CD1a Reveals T Cell Fine Specificity for Natural Lipopeptide Structures

Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit

Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

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SOLID‐PHASE PEPTIDE SYNTHESIS USING MILD BASE CLEAVAGE OF N_αFLUORENYLMETHYLOXYCARBONYLAMINO ACIDS, EXEMPLIFIED BY A SYNTHESIS OF DIHYDROSOMATOSTATIN