Antiparallel Self-Association of a ,-Hybrid Peptide: More Relevance of Weak Interactions

作者：Venugopalan Paloth; Kishore Raghuvansh^*

来源：Chemistry-An Asian Journal, 2015, 10(8): 1753-1760.

DOI：10.1002/asia.201500373

• foldamers
• peptide design
• self-association
• weak interactions
• X-ray diffraction
• -strand mimics

To learn how a preorganized peptide-based molecular template, together with diverse weak non-covalent interactions, leads to an effective self-association, we investigated the conformational characteristics of a simple ,-hybrid model peptide, Boc--Abz-Gly-OMe. The single-crystal X-ray diffraction analysis revealed the existence of a fully extended -strand-like structure stabilized by two non-conventional C-HO=C intramolecular H-bonds. The 2D (HNMR)-H-1 ROESY experiment led us to propose that the flat topology of the urethane--Abz-amide moiety is predominantly preserved in a non-polar environment. The self-association of the energetically more favorable antiparallel -strand-mimic in solid-state engenders an unusual flight of stairs' fabricated through face-to-face and edge-to-edge ArAr interactions. In conjunction with FT-IR spectroscopic analysis in chloroform, we highlight that conformationally semi-rigid -Abz foldamer in appositely designed peptides may encourage unusual -strand or -sheet-like self-association and supramolecular organization stabilized via weak attractive forces.

• 出版日期2015-8