Removing the C-terminal protecting group enlarges the crystal size: Z–(Gly–Aib)2–OH·H2O
| Autor: | Kyriacos Petratos, Hans Brückner, Renate Gessmann |
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| Rok vydání: | 2020 |
| Předmět: |
Tetrapeptide
010405 organic chemistry Hydrogen bond Chemistry Intermolecular force Crystal structure 010402 general chemistry Condensed Matter Physics 01 natural sciences 0104 chemical sciences Inorganic Chemistry Crystal Crystallography Intramolecular force Materials Chemistry Molecule Physical and Theoretical Chemistry Protecting group |
| Zdroj: | Acta Crystallographica Section C Structural Chemistry. 76:1057-1061 |
| ISSN: | 2053-2296 |
| DOI: | 10.1107/s2053229620014254 |
| Popis: | The achiral tetrapeptide monohydrate N-(benzyloxycarbonyl)glycyl-α-aminoisobutyrylglycyl-α-aminoisobutyric acid monohydrate, Z–Gly–Aib–Gly–Aib–OH·H2O (Z is benzyloxycarbonyl, Aib is α-aminoisobutyric acid and Gly is glycine) or C20H28N4O7·H2O, exhibits two conformations related by the symmetry operation of an inversion centre. It adopts only one of two possible intramolecular hydrogen bonds in a type I (and I′) β-turn and forms a maximum of intermolecular hydrogen bonds partly mediated by water. The space group, the molecular structure and the crystal packing differ from two already described (Gly–Aib)2 peptides which vary only in the protecting groups. This structure confirms the high structural flexibility of Gly–Aib peptides and points to a strong relationship between intermolecular hydrogen bonding and crystal quality and size. |
| Databáze: | OpenAIRE |
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