Base catalyzed aminolysis of carbodithioic esters and its interest in solid phase sequential analysis of peptides

Previero, A.; Gourdol, A.; Derancourt, Jean; Coletti-Previero, Maria-Antonia

doi:10.1016/0014-5793(75)80856-8

Cited by 17 publications

(4 citation statements)

References 9 publications

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“…Their employed procedure requires the polymer to be reacted with a functional azo-initiator after isolation of the polymer. 11 In addition, dithioesters and trithiocarbonates may undergo aminolysis 12,13 and hydrolysis 14 to yield thiol functional polymer. When methacrylates are employed, they can undergo intramolecular cyclization to form thiolactone end-groups.…”

Section: Introductionmentioning

confidence: 99%

Facile conversion of RAFT polymers into hydroxyl functional polymers: a detailed investigation of variable monomer and RAFT agent combinations

et al. 2010

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We report the systematic investigation of a recently introduced one-pot radical transformation of methacrylate and acrylate-type polymers prepared via reversible addition fragmentation chain transfer (RAFT) polymerization into hydroxyl functional polymers. The simple reaction procedure involves stirring a solution of the RAFT functional polymer and an azo-initiator in tetrahydrofuran at elevated temperatures (T ¼ 60 C) in the presence of ambient air. Subsequent reduction of the formed hydroperoxide functional polymers to hydroxyl functional polymers is achieved in a one-pot procedure using triphenylphosphine. Polymers investigated in the current study are poly(methyl acrylate) (pMA), poly(butyl acrylate) (pBA), poly(isobornyl acrylate) (piBoA) and poly(tert-butyl acrylate) (ptBA) carrying a dithiobenzoate or phenyldithioacetate end terminius as well as a symmetrical trithiocarbonate mid chain function. Quantitative conversion into the hydroperoxyl and hydroxyl terminated product is observed when trithiocarbonate functional polymers are employed. In the case of dithiobenzoate and phenyldithioacetate functional acrylic polymers, some minor side products due to the oxidation of the RAFT end-group are generated. Size exclusion chromatography (SEC) and size exclusion chromatography-electrospray mass spectrometry (SEC-ESI-MS) were employed to monitor the progress of the reaction and to investigate the proposed reaction mechanism for the model polymers. When trithiocarbonate functional polymers are employed in the transformation reaction, the SEC analysis shows a bisection of the initial M n . Collision induced dissociation (CID) MS experiments of the intermediate reaction products were conducted to gain in-depth information about the chemical structure. The new backbone linked hydroxyl group provides a versatile anchor for chemical end-group conversions and conjugation reactions with RAFT prepared polymers, alleviating problems with the rather limited ability of the dithioester end-group to undergo non-radical transformations.

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Section: Introductionmentioning

confidence: 99%

Facile conversion of RAFT polymers into hydroxyl functional polymers: a detailed investigation of variable monomer and RAFT agent combinations

et al. 2010

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“…Our preliminary reports in enzyme modification using dithioesters ( thioacylation ) concerned grafting reactions of either amphililic poly(ethylene oxide) oligomers or hydrophobic alkyl chains or phenyl rings. , This new method for protein chemical modification is based on the known thioacylation of primary and secondary amines by dithioesters and dithio acids which proceeds rapidly at room temperature and was originally applied to esters of amino acids or dipeptides in order to promote a new protecting group . As the back-pathway from thioacylated products to free amino groups could not be easily performed at that time, the use of thioacylating reagents as protecting groups during peptide syntheses or reactions was rapidly eliminated . However, these older works have suggested the use of dithioesters as protein thioacylating agents.…”

Section: Introductionmentioning

confidence: 99%

“…3 As the back-pathway from thioacylated products to free amino groups could not be easily performed at that time, 4 the use of thioacylating reagents as protecting groups during peptide syntheses or reactions was rapidly eliminated. 5 However, these older works have suggested the use of dithioesters as protein thioacylating agents.…”

Section: Introductionmentioning

confidence: 99%

Protein Thioacylation: 2. Reagent Stability in Aqueous Media and Thioacylation Kinetics

et al. 2000

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Several thioacylating reagents have been tested toward hydrolysis under conditions suitable for protein modifications: 20-35 degrees C and buffered solutions at pH 7.5-8.5. Aliphatic dithioesters are sufficiently stable in aqueous media at room temperature (or below) if protein modification reaction time does not exceed 24 h, whereas at 35 degrees C reaction times must be limited to a few hours. Kinetic data obtained in gelatin thioacylation at room temperature using aliphatic dithioesters and dithio acid are consistent with a second-order reaction rate with respect to amine concentration. The pH dependence of the second-order reaction rate constants indicate that dithioester reacts exclusively with the free amine form of lysine residue, whereas dithiocarboxylate ion reacts with both amine and ammonium ion, probably through a more complex mechanism. Interestingly thioacylation using dithio acids may be obtained in pH near neutrality or in slightly acidic media, thus offering protein modification possibilities at pH 5-9. Thioacylation reaction rates may be expressed as R = -(dAt/dt) = k[H3O+](-b)At2[thioacylating agent] in which At is the amine concentration at time t, constants k and b depending on the reagent nature.

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“…The use of phenylisothiocyanate (Edman reagent) as a stepwise-degradation reagent for amino acids from peptides or proteins has been one of the most useful methods of amino acid-sequence determination (Edman, 1950;Edman & Begg, 1967;Laursen, 1971). Although several new reagents (Barrett & Leigh, 1975;Previero et al, 1975) and new techniques (Morris et al, 1971;Bradbury et al, 1974;Priddle et al, 1976) have been developed, none is in widespread use to date.…”

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confidence: 99%

High-sensitivity sequence analysis of peptides and proteins by 4-NN-dimethylaminoazobenzene 4′-isothiocyanate

Chang¹

1977

Biochemical Journal

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A manual high-sensitivity sequencing method is described, in which 4-NN-dimethylaminoazobenzene 4'-isothiocyanate is used for the stepwise degradation of amino acid residues from the peptides. The 4-NN-dimethylaminoazobenzene 4'-thiazolinones of amino acids that were released, after conversion into their thiohydantoin derivatives, were identified by t.l.c. on polyamide sheets. This new method is simple and sensitive, and requires only 2-10nmol of peptides or proteins for extended sequence analysis. The method was tested on the sequence analysis of a hexapeptide (Leu-Trp-Met-Arg-Phe-Ala), bradykinin, glucagon and native lysozyme. Results show that the proposed procedure is a sensitive method for the sequence determination of short peptides as well as for the partial sequence determination of intact proteins.

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Base catalyzed aminolysis of carbodithioic esters and its interest in solid phase sequential analysis of peptides

Cited by 17 publications

References 9 publications

Facile conversion of RAFT polymers into hydroxyl functional polymers: a detailed investigation of variable monomer and RAFT agent combinations

Facile conversion of RAFT polymers into hydroxyl functional polymers: a detailed investigation of variable monomer and RAFT agent combinations

Protein Thioacylation: 2. Reagent Stability in Aqueous Media and Thioacylation Kinetics

High-sensitivity sequence analysis of peptides and proteins by 4-NN-dimethylaminoazobenzene 4′-isothiocyanate

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