Helical Porous Protein Mimics

Published

August 12, 2004

Author(s)

Virgil Percec, A E. Dulcey, Y Miura, U Edlund, V S. Balagurusamy, Steven Hudson, Paul A. Heiney, H Duan, S N. Magonov

Abstract

Pore forming proteins, peptides and their remodeled structures perform a diversity of biological and biologically inspired functions. They include viral helical coats,1 transmembrane channels2,3, mediated protein folding4 and reversible encapsulation5, stochastic sensing6, and bacterial7 and antibacterial activity8. This diversity is endowed by a combination of pore architecture that determines transport and by the surface protein structure that encodes self-assembly as mammalian or bacterial transmembranes. Nonbiological porous peptides with variable pore diameter and exterior functionality are most successfully self-assembled by a strategy that involves chirality directed H-bonding of cyclic D,L-peptides9. Biologically inspired methods to assemble nonbiological porous assemblies have not yet generated lattice self-organizable supramolecular structures that are stable both in solution and in bulk, as in the case of porous proteins and peptides10-15.This makes them unsuitable for detailed structural and design analysis by X-ray and other diffraction techniques, restricts their solution- and eliminates bulk-derived applications. Here we report the discovery of a library of amphiphilic dendritic dipeptides [(4-3,4-3,5)nG2-CH2-[Boc(MeO)-L(D)-Tyr-L(D)-Ala-OMe] (where n is the number of carbons in their alkyloxy groups, n=6 to 16) that self-assemble in solution, in film and in bulk into helical porous columns via principles resembling those of viral helical coats. The universality of this simple strategy that includes retrostructural analysis by X-ray analysis provides access to design of porous columns with variable pore diameter (8.6 to 14.4 ), pore and external surface functionalities. This will facilitate a variety of biologically inspired functions ranging from transmembrane channel mimics and antimicrobials to selective membranes.

Citation

Nature

Volume

430

Issue

7001

Pub Type

Journals

Download Paper

Local Download

Keywords

biomimicry, molecular pores, nanotechnology

Citation

Percec, V. , Dulcey, A. , Miura, Y. , Edlund, U. , Balagurusamy, V. , Hudson, S. , Heiney, P. , Duan, H. and Magonov, S. (2004), Helical Porous Protein Mimics, Nature, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=852293 (Accessed December 2, 2024)