5 years ago

C11/C9 Helical Folding in αβ Hybrid Peptides Containing 1-Amino-cyclohexane acetic acid (β3, 3-Ac6c)

C11/C9 Helical Folding in αβ Hybrid Peptides Containing 1-Amino-cyclohexane acetic acid (β3, 3-Ac6c)
Naiem Ahmad Wani, Rajkishor Rai, Umesh Prasad Singh, Srinivasarao Raghothama
The present study describes the solid-state conformation of αβ hybrid peptides, Boc-Leu-β3, 3-Ac6c-OH, P1; Boc-Leu-β3, 3-Ac6c-Leu-β3, 3-Ac6c-OMe, P2; and Boc-Leu-β3, 3-Ac6c-Leu-β3, 3-Ac6c-Leu-OMe, P3. The dipeptide P1 adopts extended conformations, whereas tetrapeptide P2 and pentapeptide P3 favor a helical conformation stabilized by mixed types of C11/C9 intramolecular hydrogen bonds. In peptide P3, the amino group of β3, 3-Ac6c(2) and β3, 3-Ac6c(4) residues occupies axial orientation, whereas in P2 it occupies axial and equatorial orientations for residues β3, 3-Ac6c(2) and β3, 3-Ac6c(4), respectively. The self-assembly of P3 forms channels filled with solvent molecules that present interesting patterns. Stable helices: Mixed C11/C9 intramolecular hydrogen bonds with opposite directionalities stabilize the helical conformation in αβ hybrid peptides.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/chem.201700265

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