Related Experiment Video
Updated: May 28, 2025

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
Published on: August 2, 2012
Interface flexibility controls the nucleation and growth of supramolecular networks
Vincenzo Caroprese1, Cem Tekin1, Veronika Cencen2
1Programmable Biomaterials Laboratory, Institute of Materials, School of Engineering, Ecole Polytechnique Fédérale Lausanne, Lausanne, Switzerland.
Abstract:
Supramolecular networks are abundantly present in nature and, like crystalline materials, often develop from an initial nucleation site, followed by growth based on directional interactions between components. Traditionally, the binding strength and directionality of interactions is thought to dictate nucleation and crystal growth, whereas structural flexibility favours defects. Usually, macromonomers present multiple binding sites with relative intramolecular flexibility, but the effects of such flexibility on regulating network formation have been given little attention. Here we introduce the concept of 'interface flexibility' and demonstrate its critical importance in the nucleation and growth of supramolecular networks. As a model system, we use trisymmetric DNA-based macromonomers, which organize into hexagonal networks through weak π-π interactions at their tips. The directional nature and low spatial tolerance of π-π interactions mean that small shifts in orientation have a large effect on effective valency. We show that too much interface flexibility disrupts network formation, regardless of affinity. Tuning the interface flexibility greatly expands the available design space for synthetic supramolecular materials.
Related Concept Videos
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Membrane Fluidity
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
Protein Folding
Protein-protein Interfaces
Ziegler–Natta Chain-Growth Polymerization: Overview
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...

