An adaptable peptide-based porous material.
Porous materials find widespread application in storage, separation, and catalytic technologies. We report a crystalline porous solid with adaptable porosity, in which a simple dipeptide linker is arranged in a regular array by coordination to metal centers. Experiments reinforced by molecular dynamics simulations showed that low-energy torsions and displacements of the peptides enabled the available pore volume to evolve smoothly from zero as the guest loading increased. The observed cooperative feedback in sorption isotherms resembled the response of proteins undergoing conformational selection, suggesting an energy landscape similar to that required for protein folding. The flexible peptide linker was shown to play the pivotal role in changing the pore conformation.
Rabone
J
J
Department of Chemistry, University of Liverpool, Liverpool, L69 7ZD, UK.
Yue
Y-F
YF
Chong
S Y
SY
Stylianou
K C
KC
Bacsa
J
J
Bradshaw
D
D
Darling
G R
GR
Berry
N G
NG
Khimyak
Y Z
YZ
Ganin
A Y
AY
Wiper
P
P
Claridge
J B
JB
Rosseinsky
M J
MJ
D000327:Adsorption; D002245:Carbon Dioxide / Q000737:chemistry*; D055598:Chemical Phenomena; D003460:Crystallization; D004058:Diffusion; D004151:Dipeptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D015394:Molecular Structure; D016062:Porosity; D011312:Pressure; D011487:Protein Conformation; D017510:Protein Folding; D012997:Solvents; D013816:Thermodynamics; D014961:X-Ray Diffraction; D015032:Zinc / Q000737:chemistry*
D004151:Dipeptides; D008024:Ligands; D012997:Solvents; D002245:Carbon Dioxide; C065992:N-glycylalanine; D015032:Zinc