Succinimide Derivative

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Sante Capasso - One of the best experts on this subject based on the ideXlab platform.

  • Effect of lysine residues on the deamidation reaction of asparagine side chains.
    Biopolymers, 2000
    Co-Authors: Sante Capasso, Gianfranco Balboni, Paola Di Cerbo
    Abstract:

    The effect of lysine residues on the deamidation reaction of the asparagine side chain has been studied on the peptide and on its lysine-acetylated Derivative in a wide range of pH values. The amino acid sequence of these peptides is similar to the local sequence flanking the labile Asn-67 in RNAse A. The experimental data show that Lys influences both the deamidation rate and the relative yield of the two reaction products, i.e., the aspartic acid and β-aspartic acid containing peptide. These effects are pH dependent and can be rationalized based on the mechanism previously proposed for the deamidation reaction via Succinimide Derivative. © 2000 John Wiley & Sons, Inc. Biopoly 53: 213–219, 2000

  • thermodynamic parameters of the reversible isomerization of aspartic residues via a Succinimide Derivative
    Thermochimica Acta, 1996
    Co-Authors: Sante Capasso
    Abstract:

    Abstract Values of the thermodynamic quantities ΔH ° and ΔS ° for the reactions “Asp-peptide ⇆ Asupeptide ⇆ β-Asp-peptide” in aqueous solution have been obtained for the model peptides AcGlyXGlyGlyNHMe and AcXGlyNHMe (X  Asp, β-Asp, Asu; Asu = aminosuccinyl residue) from the temperature-dependence of equilibrium constants. The ΔH ° and ΔS ° values for the cyclization reactions of the carboxylic-acid form of the Asp and β-Asp side chains of the dipeptides and tetrapeptides are positive and coincident within experimental error. Medium values are 34 kJ mol −1 and 127 J K −1 mol −1 for ΔH ° and ΔS °, respectively. The molar enthalpies and molar entropies of the Asp-dipeptide and β-Asp-dipeptide, and of the Asp-tetrapeptide and β-Asp-tetrapeptide, did not exhibit significant differences.

  • Kinetics and mechanism of Succinimide ring formation in the deamidation process of asparagine residues
    Journal of The Chemical Society-perkin Transactions 1, 1993
    Co-Authors: Sante Capasso, Lelio Mazzarella, Adriana Zagari, Filomena Sica, Severo Salvadori
    Abstract:

    The cyclization of Ac–Gly–Asn–Gly–Gly–NHMe to the Succinimide Derivative has been studied in the pH range 5.5–10.4 at 37° and µ= 1 mol dm–3. Kinetic evidence indicates that the reaction is a multistep process with a change in the rate-determining step at pH 6.5–7.0.The suggested mechanism involves the pre-equilibrium deprotonation of the NH group next to the Asn residue, followed by nucleophilic attack of the nitrogen atom on the carbonyl carbon of the Asn side chain giving a cyclic tetrahedral intermediate. At acidic pH the cyclization step is rate determining, whereas, the removal of the leaving group by apparent general-base catalysis is the rate-determining step at neutral and basic pH. The literature data on the deamidation rate are discussed in light of the proposed mechanism.

  • spontaneous cyclization of the aspartic acid side chain to the Succinimide Derivative
    Journal of The Chemical Society Chemical Communications, 1992
    Co-Authors: Sante Capasso, Lelio Mazzarella, F Sica, Adriana Zagari, Severo Salvadori
    Abstract:

    At equilibrium in acidic solution the Succinimide Derivative, formed by cyclization reaction of the Asp side chain, predominates; at a pH close to the apparent pKa of the Asp residue this reaction is relatively fast with a t1/2 of a few days.

Ewa Marzęda - One of the best experts on this subject based on the ideXlab platform.

Magdalena Florek-luszczki - One of the best experts on this subject based on the ideXlab platform.

Sergey L. Kocharov - One of the best experts on this subject based on the ideXlab platform.

Maria W. Kondrat-wróbel - One of the best experts on this subject based on the ideXlab platform.