35748-51-7Relevant articles and documents
A study to develop platinum(iv) complex chemistry for peptide disulfide bond formation
Huo, Shuying,Shen, Shigang,Song, Changying,Sun, Jingjing,Zhao, Xiaowei
supporting information, p. 1736 - 1741 (2020/02/20)
Platinum(iv) complexes with a heterocyclic ligand and an ancillary ligand have been investigated and applied for treating various tumour cell lines. Another application of the Pt(iv) complexes in forming peptide disulfide bonds was investigated in this work. For development of Pt(iv) complex chemistry for disulfide bond formation in peptides, two Pt(iv) complexes, [PtCl2(phen)(en)]Cl2 and [PtCl2(bpy)(en)]Cl2, were synthesized and characterized using elemental analysis, ESI-MS and NMR. Subsequently, they were investigated as oxidants for the formation of disulfide bonds in various peptides. Excellent purities and yields of disulfide-containing peptides were achieved when the reactions were carried out in aqueous solution. The reactions were completed rapidly in a wide range of pH values even in acidic medium at room temperature. An intramolecular disulfide bond was formed in each of the peptides in a solution containing two dithiol-containing peptides, making the Pt(iv) complexes useful for generating disulfide-containing peptide libraries. In addition, the two Pt(iv) complexes can be used as oxidants for the synthesis of disulfide bonds on a resin, which is a more convenient method to synthesize disulfide-containing peptides through automation.
Discovery of a highly selective and efficient reagent for formation of intramolecular disulfide bonds in peptides
Shi, Tiesheng,Rabenstein, Dallas L.
, p. 6809 - 6815 (2007/10/03)
We have discovered that trans-[Pt(en)2Cl2]2+ (en = ethylenediamine) is a highly selective and efficient reagent for the quantitative formation of intramolecular disulfide bonds in peptides. A series of 14 dithiol peptides which form disulfide-containing rings ranging in size from 14 to 53 atoms were used to characterize the reagent. The dithiol peptides are cleanly and rapidly converted to their disulfide forms by a slight excess of the platinum complex under mild reaction conditions (slightly acidic and neutral media). For all the dithiol peptides studied, including a penicillamine-derived peptide, the oxidation yields range from 97% to 100%. No side reactions were observed, including no oxidation of the methionine side chain. The reaction kinetics for oxidation of reduced pressinoic acid were found to be second order overall: rate = k'[Pt(IV)][dithiol peptide], where k' is a pH-dependent second-order rate constant. Values of 0.60 ± 0.01, 3.5 ± 0.2, and 22 ± 1 M-1 s-1 were determined for k' at pH 3.0, 4.0, and 5.0, respectively (25 °C and 0.45 M ionic strength). A reaction mechanism for oxidation of dithiol peptides by [Pt(en)2Cl2]2+ is proposed. [Pt(en)2Cl2]2+ and its reduction product [Pt(en)2]2+ are essentially substitution inert under the conditions used for disulfide formation, they are nontoxic, and they are readily separated from peptides by HPLC. The characteristics of [Pt(en)2Cl2]2+ and its reaction properties with dithiol peptides suggest that [Pt(en)2Cl2]2+ is a universal reagent for the rapid and quantitative formation of intramolecular disulfide bonds in peptides.
SYNTHESIS OF PRESSINOIC ACID BY ENZYMATICALLY CATALYZED FORMATION OF PEPTIDE BONDS
Cerovsky, Vaclav
, p. 1352 - 1360 (2007/10/02)
Three fully enzymatic syntheses of the 1-6 vasopressin hexapeptide were investigated using papain, α-chymotrypsin and thermolysin.Best results were obtained with thermolysin in the 2 + 4 fragment condensation.The α-chymotrypsin-catalysed 3 + 3 condensatio
