73607-68-8Relevant academic research and scientific papers
Solar and Visible Light Assisted Peptide Coupling
Mishra, Abhaya K.,Parvari, Galit,Santra, Sourav K.,Bazylevich, Andrii,Dorfman, Ortal,Rahamim, Jonatan,Eichen, Yoav,Szpilman, Alex M.
, p. 12406 - 12412 (2021/04/05)
Amino acid and peptide couplings are widely used in fields related to pharma and materials. Still, current peptide synthesis continues to rely on the use of expensive, water sensitive, and waste-generating coupling reagents, which are often prepared in mu
Stable β-sheet formation and enhanced hydrolytic catalysis of a sequential alternating amphiphilic polypeptide containing catalytic triads in a serine protease
Fukushima
, p. 431 - 439 (2007/10/03)
The alternating amphiphilic copolypeptide poly(Asp-Leu-His-Leu-Ser-Leu) was prepared by the synthesis and polymerization of the respective hexapeptide in order to obtain a stable β-sheet polypeptide with hydrolytic catalytic activity, like that of a serine protease. The conformation and conformational transitions in aqueous solution and in water-organic solvent mixtures were determined by circular dichroism measurements. The polypeptide reveals a very strong tendency to adopt a β-sheet structure, which is accomplished at below pH 10.0, and even by adding sodium chloride or various alcohols. However, a partial α-helical conformation is observed in an aqueous solution at pH 12.0; also, an α-helix to β-sheet conformational transition occurs upon adding 1 M NaCl. The polypeptide is a more effective catalyst than the peptide hexamer, the amino acids mixture, or imidazole for the hydrolysis of p-nitrophenyl derivatives, and catalyzed the hydrolytic reaction of the substrates more effectively with increasing their hydrophobicity. It is likely that the enhanced hydrolytic catalyst of the polypeptide may be responsible for increasing the nucleophilicity by the electrostatic interactions or condensation effect of the substrates by hydrophobic interactions. The polypeptide would make good models for constructing novel proteins with catalytic properties involving β-sheet structures.
Design of the Synthetic Route for Peptides and Proteins Based on the Solubility Prediction Method. I. Synthesis and Solubility Properties of Human Proinsulin C-Peptide Fragments
Narita Mitsuaki,Ogura, Toshihiko,Sato, Kazuhiro,Honda, Shinya
, p. 2433 - 2438 (2007/10/02)
The usefulness of the solubility prediction method is demonstrated using relatively small peptide fragments of human proinsulin C-peptide.The propriety of the solubility prediction method for peptides having polar side chains is also examined in the following respects: (1) Peptide intermediates smaller than a heptapeptide have high solubility regardless of their c> values; (2) the c> values of peptide intermediates are useful for judging solubility of peptide intermediates equal to or larger than an octapeptide level; (3) the Pro residue in a central position of a peptide chain is effective for increasing peptide solubility; and (4) there is critical chain length for peptide insolubility caused by a β-sheet aggregation.A strategy suitable for the design of the synthetic route or human proinsulin C-peptide is subsequently discussed on the basis of the solubility prediction of peptide intermediates.
