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Nucleation of the β-hairpin structure in a linear hybrid peptide containing α-, β- and γ-amino acids

✍ Scribed by Tushar K. Chakraborty; K. Srinivasa Rao; M. Udaya Kiran; B. Jagadeesh

Publisher
Elsevier Science
Year
2008
Tongue
French
Weight
190 KB
Volume
49
Category
Article
ISSN
0040-4039

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✦ Synopsis

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-d 6 .

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Nucleation of β-hairpin structure in a p
Nucleation of β-hairpin structure in a pyrrole amino acid containing peptide
✍ Tushar K. Chakraborty; B.Krishna Mohan; S.Kiran Kumar; Ajit C. Kunwar 📂 Article 📅 2003 🏛 Elsevier Science 🌐 French ⚖ 115 KB

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-h

β-Hairpins Generated from Hybrid Peptide
β-Hairpins Generated from Hybrid Peptide Sequences Containing both α- and β-Amino Acids
✍ Hosahudya N. Gopi; Rituparna S. Roy; Srinivasa R. Raghothama; Isabella L. Karle; 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 German ⚖ 342 KB 👁 1 views

The incorporation of the b-amino acid residues into specific positions in the strands and b-turn segments of peptide hairpins is being systematically explored. The presence of an additional torsion variable about the C(a)ÀC(b) bond (q) enhances the conformational repertoire in b-residues. The confor

Hybrid Peptides: Expanding the β Turn in
Hybrid Peptides: Expanding the β Turn in Peptide Hairpins by the Insertion of β-, γ-, and δ-Residues
✍ Rajkishor Rai; Prema G. Vasudev; Kuppanna Ananda; Srinivasarao Raghothama; Naray 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 441 KB

## Abstract The β turn segment in designed peptide hairpins has been expanded by the insertion of β‐, γ‐ and δ‐amino acids at the __i__+2 position. The model octapeptides Boc‐Leu‐Phe‐Val‐^D^Pro‐Ac~6~c‐Leu‐Phe‐Val‐OMe (1), Boc‐Leu‐Phe‐Val‐^D^Pro‐β^3^‐Ac~6~c‐Leu‐Phe‐Val‐OMe (2), and Boc‐Leu‐Phe‐Val‐^