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First crystallographic signature of the highly ordered supramolecular helical assemblage from a tripeptide containing a non-coded amino acid
- Source :
-
Tetrahedron Letters: International Organ for the Rapid Publication of Preliminary Communications in Organic Chemistry . Apr2002, Vol. 43 Issue 14, p2653. 4p. - Publication Year :
- 2002
-
Abstract
- The model tripeptide Boc-Leu(1)-Aib(2)-Phe(3)-OMe 1 containing a non-coded amino acid residue (Aib: α-amino isobutyric acid) forms a supramolecular helical assemblage via non-covalent interactions in single crystals. The SEM image of the peptide 1 in the solid state shows the ribbon like fibrillar morphology, a characteristic feature of highly ordered aggregated fibrils like amyloid fibrils. [Copyright &y& Elsevier]
- Subjects :
- *SUPRAMOLECULAR chemistry
*PEPTIDES
*AMYLOID
Subjects
Details
- Language :
- English
- ISSN :
- 00404039
- Volume :
- 43
- Issue :
- 14
- Database :
- Academic Search Index
- Journal :
- Tetrahedron Letters: International Organ for the Rapid Publication of Preliminary Communications in Organic Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7767498
- Full Text :
- https://doi.org/10.1016/S0040-4039(02)00283-6