Sequence-Specific Unusual (1→2)-Type Helical Turns in α/β-Hybrid Peptides

Citations Over TimeTop 15% of 2008 papers

Abstract

This article describes novel conformationally ordered alpha/beta-hybrid peptides consisting of repeating l-proline-anthranilic acid building blocks. These oligomers adopt a compact, right-handed helical architecture determined by the intrinsic conformational preferences of the individual amino acid residues. The striking feature of these oligomers is their ability to display an unusual periodic pseudo beta-turn network of nine-membered hydrogen-bonded rings formed in the forward direction of the sequence by 1-->2 amino acid interactions both in solid-state and in solution. Conformational investigations of several of these oligomers by single-crystal X-ray diffraction, solution-state NMR, and ab initio MO theory suggest that the characteristic steric and dihedral angle restraints exerted by proline are essential for stabilizing the unusual pseudo beta-turn network found in these oligomers. Replacing proline by the conformationally flexible analogue alanine (Ala) or by the conformationally more constrained alpha-amino isobutyric acid (Aib) had an adverse effect on the stabilization of this structural architecture. These findings increase the potential to design novel secondary structure elements profiting from the steric and dihedral angle constraints of the amino acid constituents and help to augment the conformational space available for synthetic oligomer design with diverse backbone structures.

Related Papers

• → Disulfide Bond Dihedral Angles from Raman Spectroscopy(1973)184 cited
• → Protein Dihedral Angle Prediction: The State of the Art(2023)4 cited
• → Construction of Space-filling Models of Proteins Using Dihedral Angles(1972)8 cited
• → 2-(3,5-Dichlorophenyl)-1,4-benzoquinone(2002)2 cited
• → Dihedral angle database based on disulfide bonds(2004)1 cited