A modified benzhydrylamine - A useful handle reagent for Fmoc based solid phase synthesis of peptide amides

Usefulness of a dimethoxybenzhydrylamine derivative, 3-(3-(Fmoc-amino-4-methoxyphenylmethyl)-4-methoxyphenyl)propionic acid, for Fmoc-based solid phase synthesis of peptide amides was demonstrated by preparation of three biologically active peptide amides, i.e. tetragastrin, neuromedin B and [8-arginine]vasopressin. 1M trimethylsilyl bromide-thioanisole (molar ratio 1 : 1) in trifluoroacetic acid was recommended as a deprotecting reagent for releasing the peptide amides from the resin.

Download Full-text

Direct Solid Phase Synthesis of Biologically Active Peptide Alcohols

Journal of the Chinese Chemical Society ◽

10.1002/jccs.199900020 ◽

1999 ◽

Vol 46 (2) ◽

pp. 135-138 ◽

Cited By ~ 3

Author(s):

Ying-Ta Wu ◽

Hsing-Pang Hsieh ◽

Shui-Tein Chen ◽

Kung-Tsung Wang

Keyword(s):

Solid Phase Synthesis ◽

Solid Phase ◽

Biologically Active ◽

Phase Synthesis ◽

Active Peptide ◽

Biologically Active Peptide ◽

Direct Solid

Download Full-text

Synthesis of [1-β-mercaptopropionic acid, 8-D-arginine]vasopressin (DDAVP) in solid phase. Simple optimalization

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19791173 ◽

1979 ◽

Vol 44 (4) ◽

pp. 1173-1178 ◽

Cited By ~ 4

Author(s):

Viktor Krchňák ◽

Milan Zaoral

Keyword(s):

Arginine Vasopressin ◽

Solid Phase Synthesis ◽

Solid Phase ◽

Experimental Conditions ◽

Phase Synthesis ◽

Mercaptopropionic Acid ◽

Better Than

A series of solid-phase syntheses of the protected precursor II of DDAVP was carried out. Experimental conditions were developed under which practically pure II can reproducibly be obtained in yields better than 60%. The protected precursors of DDAVP obtained by liquid- and solid-phase synthesis and DDAVP samples obtained from these precursors were undistinguishable by conventional analytical or pharmacological assays.

Download Full-text

Festphasensynthese von Muramyldipeptiden an isomeren Trialkoxybenzylamin-Harzen / Solid Phase Synthesis of Muramyl Dipeptides on Isomeric Trialkoxybenzylamine Resins

Zeitschrift für Naturforschung B ◽

10.1515/znb-1998-0716 ◽

1998 ◽

Vol 53 (7) ◽

pp. 753-764 ◽

Cited By ~ 1

Author(s):

Hans-Jürgen Kohlbaua ◽

Jochen Tschakert ◽

Raed A. Al-Qawasmeh ◽

Tanveer Ahmad Nizamì ◽

Abdul Malik ◽

...

Keyword(s):

Amino Acids ◽

Trifluoroacetic Acid ◽

Solid Phase Synthesis ◽

Solid Phase ◽

Subsequent Treatment ◽

Phase Synthesis ◽

Merrifield Resin

Abstract New isomeric trialkoxybenzylamine resins are developed coupling phthalimidomethyl-3,5-dimethoxyphenols to the Merrifield resin, followed by subsequent treatment with hydrazine. The generated benzylamine function allows DCC coupling w ith the carboxyl function of amino acids and peptides which are removed as amides after treatment with trifluoroacetic acid. These new trialkoxybenzylamine resins allow expeditious syntheses of peptide amides and glycopeptide amides as is demonstrated for muramyl peptides and analogues.

Download Full-text

A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, DL-2-amino-3-(7-methoxy-4-coumaryl)propionic acid

Biochemical Journal ◽

10.1042/bj2740045 ◽

1991 ◽

Vol 274 (1) ◽

pp. 45-48 ◽

Cited By ~ 27

Author(s):

C G Knight

Keyword(s):

Amino Acid ◽

Propionic Acid ◽

Model Compound ◽

Solid Phase Synthesis ◽

Solid Phase ◽

Fluorescent Substrate ◽

Peptide Substrates ◽

Phase Synthesis ◽

Fluorescent Peptide ◽

Fluorescent Amino Acid

DL-2-Amino-3-(7-methoxy-4-coumaryl)propionic acid, a new fluorescent amino acid (abbreviated to Amp), has been synthesized to provide an alternative to tryptophan in quenched fluorescent peptide substrates for peptidases. The model compound Ac-DL-Amp-NH2 was intensely fluorescent with an excitation maximum at 328 nm and an emission maximum at 392 nm. Fmoc (fluoren-9-ylmethoxycarbonyl)-DL-Amp was made to allow the solid-phase synthesis of Amp-containing peptides by the Fmoc-polyamide method. The peptide derivative Dnp (2,4-dinitrophenyl)-Pro-Leu-Gly-Pro-DL-Amp-D-Lys was cleaved by thimet peptidase at the Leu-Gly bond, with a 20-fold enhancement of fluorescence. The value of kcat./Km for thimet peptidase was 6.7 x 10(5) M-1.s-1, compared with the value of 2.4 x 10(5) M-1.s-1 for the tryptophan-containing analogue, Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys.

Download Full-text