期刊
SUPRAMOLECULAR CHEMISTRY
卷 20, 期 7, 页码 625-633出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/10610270701565194
关键词
self-assembly; supramolecular helix; supramolecular beta-sheet; peptides; filaments; ribbon
资金
- Senior Research Fellowship
- University of Calcutta
- University of Reading, UK
Single crystal X-ray diffraction studies show that the beta-turn structure of tetrapeptide I, Boc-Gly-Phe-Aib-Leu-OMe (Aib: alpha-amino isobutyric acid) self-assembles to a supramolecular helix through intermolecular hydrogen bonding along the crystallographic a axis. By contrast the beta-turn structure of an isomeric tetrapeptide II, Boc-Gly-Leu-Aib-Phe-OMe self-assembles to a supramolecular beta-sheet-like structure via a two-dimensional (a, b axis) intermolecular hydrogen bonding network and pi-pi interactions. FT-IR studies of the peptides revealed that both of them form intermolecularly hydrogen bonded supramolecular structures in the solid state. Field emission scanning electron micrographs (FE-SEM) of the dried fibrous materials of the peptides show different morphologies, non-twisted filaments in case of peptide I and non-twisted filaments and ribbon-like structures in case of peptide II.
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