PubMed Health⌕ Search

PubMed · 16548570

Engineered wettability in tree capillaries.

Abstract

The water-conducting network of capillaries in plants has evolved to cope with the frequent occurrence of cavitation, which leads to air-filled capillaries that are unable to function in water transport. However, the material from which the capillaries are constructed is not perfectly wetted by water, contrary to what is often assumed and to what one might expect in an optimal design. I demonstrate that nature is able to overcome this deficiency by engineering the roughness of the capillary walls to achieve near complete wetting, a strategy analogous to that used in the natural engineering of the wettability of plant leaves and insect wings. The results provide an appealing answer to the long-standing debate on the function of wall sculpturing in plant capillaries, and may provide biomimetic clues for the engineering of wettability in technological applications such as microfluidics.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Mika M Kohonen. 2006-03-28. Engineered wettability in tree capillaries.. https://doi.org/10.1021/la052861x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Dissecting the general physicochemical properties of noncovalent interactions involving tyrosine side chain as a second-shell ligand in biomolecular metal-binding site mimetics: an experimental study combining fluorescence, 13C NMR spectroscopy and ESI mass spectrometry.

Detailed physicochemical features inherent in the dynamic cation-pi interactions of aromatic amino acid side chains in the secondary coordination spheres around metal ions were extracted and mapped by intrinsic tyrosine fluorescence titration experiments with two homologous, artificially engineered metal-binding scaffolds which mimic metal-binding sites in metalloproteins. A newly formulated method for the treatment of fluorescence titration data allows straightforward assessment of both the magnitudes and properties of metal-chelation-assisted cation-aromatic interactions (K2) underlying a proposed two-step metallosupramolecular association process. The unprecedented linear platform-motif correlations between the two contrasting scaffolds in their changes in tyrosine fluorescence on binding of 3d metal cations help to elucidate the properties of general cation-arene recognition corresponding to the metal-responsive characteristics of the second-shell Tyr residue surrounding the metal-binding sites in the supramolecular context, and thereby define a new noncovalent design principle for metal-ion recognition in aqueous solution. As supported by NMR spectroscopic and ESI-MS analyses and molecular mechanics force field calculations, the systematic study exemplifies the concept of using steady-state tyrosine fluorescence as a powerful tool for comprehensive descriptions of cation-pi interactions in the extended environment of a metal-binding site. We established that the physicochemical properties pertaining to indirect metal-arene interactions are highly dependent on the electronic properties of the metal ions. This work suggests that second-shell cation-pi interactions may play more diverse roles, including modulation of structure, reactivity, and function of metal-binding sites, than the previously well-established direct cation-pi interactions involving hard cations (e.g., alkali metal ions). Moreover, such a study will continue to complement theoretical predications and/or the early experimental investigations in organic solvents.

Biomimetics↗