Foldamers to Nanotubes: Influence of Amino Acid Side Chains in the Hierarchical Assembly of α, γ4‐Hybrid Peptide Helices. Issue 50 (24th October 2014)

• Record Type: Journal Article
• Authors: Jadhav, Sandip V.; Misra, Rajkumar; Gopi, Hosahudya N.
• Is Part Of: Chemistry. Volume 20:Issue 50(2014)
• Page Start: 16523
• Page End: 16528
• Publication Date: 2014-10-24
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201404961
• Languages: English
• ISSNs: 0947-6539

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Supramolecular assembly of various artificially folded 12‐helical architectures composed of γ⁴‐Val, γ⁴‐Leu and γ⁴‐Phe residues is investigated. In contrast to the 12‐helices composed of γ⁴‐Val and γ⁴‐Leu residues, the helices with γ⁴‐Phe residues displayed unique elongated nanotubular architectures. The elongated nanotube assembly was further explored as a template for biomineralization of silver ions to silver nanowires. A comparative study using an analogous α‐peptide helix reveals the importance of the spatial arrangement of aromatic side chains along the helical cylinder in a 12‐helix. These results suggested that the proteolytically and structurally stable α, γ⁴‐hybrid peptide 12‐helices may serve as a new generation of potential templates in the design of functional biomaterials.</p> </abstract>