Preparation and Applications of Pentafluorophenyl Esters of 9-Fluorenylmethyloxycarbonyl Amino Acids for Peptide Synthesis

Kisfaludy, L.; Schön, István

doi:10.1055/s-1983-30327

Cited by 172 publications

(82 citation statements)

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“…L-Alanyl-L-alanyl-1-chloro-L-alanine and L-alanyl--chloro-L-alanine were prepared by solid-phase peptide synthesis (1). The required 9-fluoroenylmethoxycarbonyl-fi-chloro-L-alanine pentafluorophenyl ester was prepared by the general method of Kisfaludy and Schon (6). All other peptides were obtained from Sigma Chemical Company, St. Louis, Mo., or Bachem Feinchemikalien AG, Bubendorf, Switzerland.…”

Section: Methodsmentioning

confidence: 99%

Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis

et al. 1993

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). The second system is a metabolic energy-dependent oligopeptide transport system which transports peptides of four to at least six amino acid residues. The involvement of a specific oligopeptide transport system in the utilization of tetra-alanine and penta-alanine was established in a mutant of L. lactis MG1363 that was selected on the basis of resistance to toxic analogs of alanine and alanine-containing di-and tripeptides. This mutant is unable to transport alanine, dialanine, and trialanine but still shows uptake of tetra-alanine and penta-alanine. The oligopeptide transport system has a lower activity than the di-tripeptide transport system. Uptake of oligopeptides occurs in the absence of a proton motive force and is specifically inhibited by vanadate. The oligopeptide transport system is most likely driven by ATP or a related energy-rich, phosphorylated intermediate.Lactococci require, in addition to a carbohydrate source, nucleotides, vitamins (3), and amino acids (20) for growth. The actual number of amino acids required for growth is strain dependent. The amino acid requirement can be satisfied by free amino acids, peptides, and/or proteins (i.e., caseins). For degradation of proteins, lactococci possess an extracellular cell wall-bound proteinase and peptidases which act in concert to supply the cells with essential and growth-stimulating amino acids and small peptides (for reviews, see references 9 and 26). Transport of the caseinderived amino acids is mediated by several different amino acid transport systems (for a review, see reference 7).In addition to amino acid uptake, lactococci can also satisfy their amino acid demand by uptake of peptides. One uptake system specific for di-and tripeptides has been investigated in a peptidase-free membrane vesicle system (23). In that study, alanyl-glutamate (Ala-Glu) was used as a model substrate. Accumulation of the dipeptide in membrane vesicles of Lactococcus lactis ML3 fused with liposomes containing beef heart cytochrome c oxidase was found to be driven by the electrical potential (A+f) and the chemical gradient of protons (ApH) across the membrane (23). Information about the specificity of this transport system is limited and is restricted to results obtained from competition experiments in which the rate of uptake of radioactively labelled peptides was estimated in the absence or presence of a few unlabelled peptides (10,22,23 in-derived amino acids will be supplied to the cells as proline-containing peptides. The finding that especially proline-containing dipeptides are high-affinity substrates for the lactococcal di-tripeptide transport system is in agreement with this notion (24).Information about the presence and properties of transport systems for oligopeptides (peptides containing four or more amino acid residues) is virtually lacking. Growth (10) and transport (22) studies with L. lactis have indicated that the size restriction for peptide utilization is four to five amino acid residues. In this study, the presence of an oligopeptide transpor...

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Section: Methodsmentioning

confidence: 99%

Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis

et al. 1993

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“…Following the procedure described by Kisfaludy and Scho Èn [26] for the related cysteine derivative, the title compound was prepared from Fmoc-Sec(Mob)-OH [9]. Yield: 71%; homogeneous on TLC (solvent system: cyclohexane/CHCl 3 /AcOH, 9 : 9 : 2); m.p.…”

Section: Fmoc-sec(mob)-opfpmentioning

confidence: 99%

Synthesis of selenocysteine peptides and their oxidation to diselenide-bridged compounds

Besse

Moröder

1997

J. Peptide Sci.

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Using the Fmoc/tBu protection scheme and the p-methoxybenzyl derivative of selenocysteine, the synthesis of related peptides in the selenol-protected form could be optimized by operating the coupling steps in the absence of auxiliary bases and by reducing the piperidine treatment to the minimum time required for quantitative Fmoc cleavage. Under these conditions, beta-elimination of the p-methoxybenzylselenol as the main side reaction of these syntheses, as well as epimerization of the protected selenocysteine, was largely suppressed. Conversion of the selenol- and thiol-protected bis-selenocysteine and selenocysteine, cysteine peptides into the related cyclic monomeric forms by iodine-mediated oxidation failed since a complex mixture of compounds was produced. Cleavage of the selenoether bond with mercuric acetate was found to proceed smoothly, but displacement of the heavy metal ions by treatment with excesses of thiols or hydrogen sulphide was unsuccessful since a stable Hg2+ diselenide complex was obtained. However, oxidation was achieved in good yields by the dimethylsulphoxide/trifluoroacetic acid procedure and the peptides were then used for determining the redox potential of the diselenide and selenide/sulphide bridge, respectively.

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“…The first amino acid (Fmoc-Ala-OH) was coupled by the Blankemeyer-Menge procedure (Blankemeyer-Menge et al, 1990). N R -Deprotections were carried out with 20% piperidine in DMF for 10 min, and W and F were incorporated as their N R -fluoren-9-ylmethoxycarbonyl (Fmoc)-protected pentafluorophenyl (Pfp) esters (Kisfaludy & Schön, 1983) (3 equiv) with the addition of 3,4-dihydro-3-hydroxy-4-oxo-1,2,3-benzotriazine (DhbtOH, 1 equiv) (König & Geiger, 1970). The side chain of W was protected with an N-tert-butoxycarbonyl (Boc) group, and the coupling times were 2 h. The glycosylated building block N R -FmocThr(R-ManAc 4 )OPfp (Andrews & Seale, 1993) (2 equiv) was allowed to react overnight.…”

Section: Purification Of Rnase 2 and High-molecular Massmentioning

confidence: 99%

Spectroscopic and Protein Chemical Analyses Demonstrate the Presence of C-Mannosylated Tryptophan in Intact Human RNase 2 and Its Isoforms

et al. 1996

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Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789]. In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments. The evidence for the occurrence of C 2 -R-mannosyltryptophan [(C 2 -Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation. In this paper, we have (1) excluded the possibility that (C 2 -Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH >5 throughout these procedures, (2) demonstrated the occurrence of (C 2 -Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C 2 -Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated. These observations firmly establish C-mannosylation as a novel way of posttranslationally attaching carbohydrate to protein, in addition to the well-known N-and O-glycosylations. Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.

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Preparation and Applications of Pentafluorophenyl Esters of 9-Fluorenylmethyloxycarbonyl Amino Acids for Peptide Synthesis

Cited by 172 publications

References 0 publications

Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis

Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis

Synthesis of selenocysteine peptides and their oxidation to diselenide-bridged compounds

Spectroscopic and Protein Chemical Analyses Demonstrate the Presence of C-Mannosylated Tryptophan in Intact Human RNase 2 and Its Isoforms

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