Solubility of Al (Benzyloxycarbonyl)-L-Aspartyl-L-Phenylalanine Methyl Ester Forming a Complex with L-Phenylalanine Methyl Ester in Aqueous System.

Hirata, Makoto; Nemoto, Katsumi; Hirata, Akira

doi:10.1252/jcej.27.72

Cited by 8 publications

(2 citation statements)

References 9 publications

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“…The distribution ratio of F-AspPheOMe in aqueous/organic biphasic systems during its continuous extractive synthesis was higher in almost all cases. This was because the complex formation between F-AspPheOMe and cosolute (F-L-Asp, L-PheOMe, and thermoase) increased the solubility of F-AspPheOMe to the organic phase, which was probably the same phenomenon observed in the partitioning of another peptide derivative (Hirata et al, 1994). This will be an important factor in the design of industrial-scale productions of peptides utilizing an extractive reaction in an aqueous/organic biphasic system.…”

Section: Continuous Synthesis Of F-asppheome In Aqueous/organic Biphamentioning

confidence: 96%

Continuous enzymatic production of peptide precursor in aqueous/organic biphasic medium

Murakami

Yoshida²,

Hayashi³

et al. 2000

Biotechnol. Bioeng.

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Section: Continuous Synthesis Of F-asppheome In Aqueous/organic Biphamentioning

confidence: 96%

Continuous enzymatic production of peptide precursor in aqueous/organic biphasic medium

Murakami

Yoshida²,

Hayashi³

et al. 2000

Biotechnol. Bioeng.

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“…The FRET substrate Abz-MKALTLQ-EDDnp was synthesized using the solid phase synthesis method [13] according to the Fmoc procedure. An automated bench-top simultaneous multiple solid-phase peptide synthesizer (PSSM 8 system; Shimadzu) was used in the synthesis.…”

Section: Peptide Synthesismentioning

confidence: 99%

C-Npys (S-3-nitro-2-pyridinesulfenyl) and peptide derivatives can inhibit a serine-thiol proteinase activity from Paracoccidioides brasiliensis

Matsuo

Carmona

Silva

et al. 2007

Biochemical and Biophysical Research Communications

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The inhibitory capacity of C-Npys (S-[3-nitro-2-pyridinesulfenyl]) derivatives over thiolcontaining serine proteases has never been tested. In the present work we used an extracellular serine-thiol proteinase activity from the fungal pathogen Paracoccidioides brasiliensis (PbST) to describe a potent inhibitory capacity of Bzl-C(Npys)KRLTL-NH 2 and Bzl-MKRLTLC(Npys)-NH 2 . The assays were performed with PbST enriched upon affinity chromatography in a paminobenzamidine (pABA)-Sepharose column. Although PbST can cleave the fluorescence resonance energy transfer peptide Abz-MKRLTL-EDDnp between L-T, the C(Npys) derivatives were not substrates nor were they toxic in a cell detachment assay, allowing therapeutic use. The best inhibitor was Bzl-C(Npys)KRLTL-NH 2 (K i = 16 nM), suggesting that the peptide sequence promoted a favorable interaction, especially when C(Npys) was placed at a further position from the L-T bond, at the N-terminus. Inhibition was completely reverted with dithioerythritol, indicating that it was due to the reactivity of the C(Npys) moiety with a free SH-group.

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Mathematical approach to thermolysin-catalyzed synthesis of aspartame precursor

Murakami

Hirata

1996

Journal of Fermentation and Bioengineering

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Solubility of Al (Benzyloxycarbonyl)-L-Aspartyl-L-Phenylalanine Methyl Ester Forming a Complex with L-Phenylalanine Methyl Ester in Aqueous System.

Cited by 8 publications

References 9 publications

Continuous enzymatic production of peptide precursor in aqueous/organic biphasic medium

Continuous enzymatic production of peptide precursor in aqueous/organic biphasic medium

C-Npys (S-3-nitro-2-pyridinesulfenyl) and peptide derivatives can inhibit a serine-thiol proteinase activity from Paracoccidioides brasiliensis

Mathematical approach to thermolysin-catalyzed synthesis of aspartame precursor

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