Shaping quaternary assemblies of water-soluble non-peptide helical foldamers by sequence manipulation.
The design and construction of biomimetic self-assembling systems is a challenging yet potentially highly rewarding endeavour that contributes to the development of new biomaterials, catalysts, drug-delivery systems and tools for the manipulation of biological processes. Significant progress has been achieved by engineering self-assembling DNA-, protein- and peptide-based building units. However, the design of entirely new, completely non-natural folded architectures that resemble biopolymers ('foldamers') and have the ability to self-assemble into atomically precise nanostructures in aqueous conditions has proved exceptionally challenging. Here we report the modular design, formation and structural elucidation at the atomic level of a series of diverse quaternary arrangements formed by the self-assembly of short amphiphilic α-helicomimetic foldamers that bear proteinaceous side chains. We show that the final quaternary assembly can be controlled at the sequence level, which permits the programmed formation of either discrete helical bundles that contain isolated cavities or pH-responsive water-filled channels with controllable pore diameters.
Université de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|CNRS, CBMN, UMR 5248, F-33600, Pessac, France.
Gavin W
GW
Collie
Université de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|CNRS, CBMN, UMR 5248, F-33600, Pessac, France.
Karolina
K
Pulka-Ziach
Université de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|CNRS, CBMN, UMR 5248, F-33600, Pessac, France.
Caterina M
CM
Lombardo
Université de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|CNRS, CBMN, UMR 5248, F-33600, Pessac, France.
Juliette
J
Fremaux
CNRS, UMS3033/US001, Institut Européen de Chimie et Biologie, Pessac 33607, France.
Frédéric
F
Rosu
CNRS, CBMN, UMR 5248, F-33600, Pessac, France.|Université de Bordeaux, CBMN, UMR 5248, All. Geoffroy Saint-Hilaire, Pessac 33600, France.
Marion
M
Decossas
Université de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|CNRS, CBMN, UMR 5248, F-33600, Pessac, France.|UREkA Sarl, 2 rue Robert Escarpit, Pessac 33607, France.
Laura
L
Mauran
CNRS, CBMN, UMR 5248, F-33600, Pessac, France.|Université de Bordeaux, CBMN, UMR 5248, All. Geoffroy Saint-Hilaire, Pessac 33600, France.
Olivier
O
Lambert
Université de Bordeaux, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|Inserm, U869, ARNA Laboratory, 146 rue Léo Saignat, Bordeaux 33076, France.
Valérie
V
Gabelica
Université de Bordeaux, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|Inserm, U869, ARNA Laboratory, 146 rue Léo Saignat, Bordeaux 33076, France.
Cameron D
CD
Mackereth
Université de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, Pessac 33607, France.|CNRS, CBMN, UMR 5248, F-33600, Pessac, France.
Gilles
http://orcid.org/0000-0002-2584-7502
G
Guichard
D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D049329:Nanostructures; D010455:Peptides / Q000737:chemistry; D011108:Polymers / Q000737:chemistry*; D014508:Urea / Q000737:chemistry
D010455:Peptides; D011108:Polymers; D014508:Urea