The Preparation of Peptides Using Mixed Carbonic—Carboxylic Acid Anhydrides

Vaughan, James R.; Osato, Ruth L.

doi:10.1021/ja01123a028

Cited by 296 publications

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“…Our esterification and amidation of phenolic acids was a modified method of mixed anhydride method for peptide synthesis using iBocCl 34 and esterification using mixed carboxylic-carbonic anhydrides and DMAP. 35 The advantage of our method is simultaneous protection of phenolic hydroxyl group(s) on phenolic acid in the esterification and amidation.…”

Section: Resultsmentioning

confidence: 99%

One-pot esterification and amidation of phenolic acids

et al. 2014

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Section: Resultsmentioning

confidence: 99%

One-pot esterification and amidation of phenolic acids

et al. 2014

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“…NH 2 and COOH termini were protected by Boc (8) and methyl groups, respectively. Isobutyl chloroformate (9) and carbodiimide (10) condensed the monomer to a dimer and the dimer to a tetramer, respectively. The following peptide derivatives were synthesized: Boc-D-Phe, D-Phe tertbutyl ester, (D-Phe) 2 …”

Section: Methodsmentioning

confidence: 99%

An Alkaline D-Stereospecific Endopeptidase with β-Lactamase Activity from Bacillus cereus

Asano

Ito

Dairi

et al. 1996

Journal of Biological Chemistry

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. A D-peptidase has been purified and characterized from an actinomycete, although it is not strictly specific toward peptides containing D-amino acids (2). In Enterococcus, the vanX gene product, (D-Ala) 2 hydrolase, plays a role in vancomycin resistance (3). The chemically synthesized "D-enzyme" of human immunodeficiency virus type 1, in which all of the amino acids were replaced with the corresponding D-amino acids, displays D-stereospecificity (4). We discovered D-aminopeptidase (EC 3.4.11.19) from Ochrobactrum anthropi and found that its primary structure is similar to the ␤-lactamases and penicillin-binding proteins (5, 6). The enzyme acts mostly on peptides with D-Ala at the NH 2 terminus to yield D-amino acids and does not act on D-amino acid derivatives with bulkier substituents. We proposed that Daminopeptidase is a new "penicillin-recognizing enzyme" (1), based on its primary structure, inhibition by ␤-lactam compounds, and the ability to catalyze peptide bond formation in organic solvents, although the enzyme does not show ␤-lactamase activity (6, 7).In this paper, we describe the screening of soil microorganisms for D-stereospecific endopeptidases using a synthetic peptide ((D-Phe) 4 ), characterization of the new enzyme alkaline D-peptidase (ADP), 1 as well as cloning and sequencing of the adp gene from Bacillus cereus strain DF4-B. EXPERIMENTAL PROCEDURESMaterials-DEAE-Toyopearl 650 M, Butyl-Toyopearl 650 M, and HPLC G-3000 SW and ODS-80Ts columns were purchased from Tosoh Corp. (Tokyo, Japan); Superdex 200 was from Pharmacia (Uppsala); and Cosmosil 5C18-MS from Nacalai Tesque (Kyoto, Japan). Membrane filters (Diaflo Ultrafilter PM-30) and the Hollow Fiber cartridge system (Hollow Fiber Ultrafilter H10-P10) were obtained from Amicon, Inc. (Beverly, MA). Chemicals other than the peptides described below were from commercial sources and were used without further purification.Synthesis of Substrates-Peptide substrates used to screen and test the substrate specificity were synthesized from D-and L-Phe. NH 2 and COOH termini were protected by Boc (8) and methyl groups, respectively. Isobutyl chloroformate (9) and carbodiimide (10) condensed the monomer to a dimer and the dimer to a tetramer, respectively. The following peptide derivatives were synthesized:The details will be reported elsewhere. SO (10%, w/v) and then added to 2 ml of LB medium containing soil samples. The mixture was then aerobically shaken for 2 days. A loopful of the culture broth was transferred to the same medium and aerobically incubated under the same conditions. A small portion of the culture broth was streaked onto a plate of the same medium containing 1.5% agar and incubated at 30°C overnight. Strains forming clear zones around the colonies were isolated, and (D-Phe) 4 degradation in the liquid culture was monitored by TLC (chloroform/methanol/acetic acid ϭ 8:2:1 or 10:2:1) and visualized with ninhydrin. (D-Phe) n (n ϭ 1-4) were well separated by TLC with the solvent. A bacterial strain isolated from a soil of Kanagawa Pr...

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“…The compounds 1 -14 were synthesized using the mixed anhydrides method [4]. A general description of the method is given in the Experimental part of this paper.…”

Section: Chemistrymentioning

confidence: 99%

New Derivatives of Picolinic Acid and Nicotinic Acid with Anticonvulsant Activity

Paruszewski¹,

Strupińska²,

Rostafinska-Suchar³

et al. 2005

PPL

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Previously obtained Pic-BZA is a potent anticonvulsant with low neurotoxicity, but its half-time of action is only about 15 min. In search for equally effective anticonvulsants but with a longer time of action fourteen Pic-BZA analogs were obtained. The compounds were evaluated in the Anticonvulsant Screening Project (ASP) of Antiepileptic Drug Development Program (ADDP) of NIH. Picolinic acid 2-fluorobenzylamide (Pic-2-F-BZA, 7) appeared to be the most effective compound of the series.

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The Preparation of Peptides Using Mixed Carbonic—Carboxylic Acid Anhydrides

Cited by 296 publications

References 0 publications

One-pot esterification and amidation of phenolic acids

One-pot esterification and amidation of phenolic acids

An Alkaline D-Stereospecific Endopeptidase with β-Lactamase Activity from Bacillus cereus

New Derivatives of Picolinic Acid and Nicotinic Acid with Anticonvulsant Activity

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