Synthesis and conformational studies of a short linear peptide containing a pyrrole amino acid (1, Paa) and a furan amino acid (2, Faa), namely Boc-hGly-Faa-D-Pro-Gly-Paa-hGly-Faa-OMe (3), were carried out in which it was established that peptide 3 adopted a well-defined b-hairpin structure in DMSO-
Nucleation of β-hairpin structure in a pyrrole amino acid containing peptide
✍ Scribed by Tushar K. Chakraborty; B.Krishna Mohan; S.Kiran Kumar; Ajit C. Kunwar
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- French
- Weight
- 115 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0040-4039
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✦ Synopsis
Synthesis and conformational studies of two short peptides containing pyrrole amino acids (1, Paa), Boc-Paa-Paa-D-Pro-Gly-Xaa-Paa-Paa-OMe (2: Xaa=Ala; 3: Xaa=Val), were carried out in which it was established that replacement of Ala in 2 with a Val residue helps peptide 3 to adopt a well-defined b-hairpin conformation in a nonpolar solvent, like CDCl 3 .
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Single crystal X-ray diffraction study reveals that the water soluble tetrapeptide H 2 N-Ile-Aib-Leu-m-ABA-CO 2 H, containing non-coded Aib (a-amino isobutyric acid) and m-ABA (meta-amino benzoic acid), crystallizes with two smallest possible diastereomeric b-hairpin molecules in the asymmetric unit