Embodying a stable α-helical protein structure through efficient chemical ligation via thioether formation
| Autor: | Mineo Niwa, Shiroh Futaki, Tomoko Ishikawa, Kouki Kitagawa, Takeshi Yagami |
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| Rok vydání: | 1997 |
| Předmět: |
Circular dichroism
Protein Conformation Stereochemistry Molecular Sequence Data Clinical Biochemistry Pharmaceutical Science Peptide Sulfides Biochemistry Mass Spectrometry chemistry.chemical_compound Protein structure Thioether Drug Discovery Moiety Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Circular Dichroism Organic Chemistry Proteins Peptide Fragments Chaotropic agent chemistry Chromatography Gel Molecular Medicine Spectrophotometry Ultraviolet Chemical ligation |
| Zdroj: | Bioorganic & Medicinal Chemistry. 5:1883-1891 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/s0968-0896(97)00119-3 |
| Popis: | A new approach was developed to embody the alpha-helical protein structure having an arbitrary combination and arrangement of helices by the successive ligation of a haloacetyl peptide segment with a cysteinyl peptide. A four-helix-bundle protein was efficiently constructed by the repetitive ligation of alpha-helical peptide segments. The use of HPLC-purified unprotected peptide segments facilitated the purification of the intermediates to afford the highly homogeneous desired protein. The use of the bromoacetyl moiety and the chloroacetyl moiety for the ligation was judged to make no difference in practice. A trial of introducing an additional intramolecular disulfide cross-link was also examined. The resulting protein showed high stability in the chaotropic and thermal denaturation and in enzymatic degradation. |
| Databáze: | OpenAIRE |
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