Peptide α-helics for synthetic nanostructures

MG Ryadnov

Research output: Contribution to journalArticle (Academic Journal)peer-review

17 Citations (Scopus)


Supramolecular structures arising from a broad range of chemical archetypes are of great technological promise. Defining such structures at the nanoscale is crucial to access principally new types of functional materials for applications in bionanotechnology. In this vein, biomolecular self-assembly has emerged as an efficient approach for building synthetic nanostructures from the bottom up. The approach predominantly employs the spontaneous folding of biopolymers to monodisperse three-dimensional shapes that assemble into hierarchically defined mesoscale composites. An immediate interest here is the extraction of reliable rules that link the chemistry of biopolymers to the mechanisms of their assembly. Once established these can be further harnessed in designing supramolecular objects de novo. Different biopolymer classes compile a rich repertoire of assembly motifs to facilitate the synthesis of otherwise inaccessible nanostructures. Among those are peptide a-helices, ubiquitous folding elements of natural protein assemblies. These are particularly appealing candidates for prescriptive supramolecular engineering, as their well-established and conservative design rules give unmatched predictability and rationale. Recent developments of self-assembling systems based on helical peptides, including fibrous systems, nanoscale linkers and reactors will be highlighted herein.
Translated title of the contributionPeptide α-helics for synthetic nanostructures
Original languageEnglish
Pages (from-to)487 - 491
Number of pages5
JournalBiochemical Society Transactions
Volume35 (3)
Publication statusPublished - Jun 2007

Bibliographical note

Publisher: Portland Press


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