Amino-Acid-Based Metallo-Hydrogel That Acts Like an Esterase.
Kousik GayenKingshuk BasuDipayan BairagiValeria CastellettoIan William HamleyArindam BanerjeePublished in: ACS applied bio materials (2018)
A histidine-based amphiphile containing a C14 fatty acyl chain, N- histidyl N'-myristry ethyl amine ( AM1 , 14.7 mM) forms hydrogels in the presence of Fe 3+ (within the range 1.47 to 4.41 mM) and Hg 2+ (within the range 3.67 to 11.02 mM) ions in aqueous dispersions at pH 6.6 (27 °C). The imidazole ring of the histidine residue plays a vital role to interact with these metal-ions. The thermal and mechanical stability of these metallo-hydrogels can be tuned by changing the proportion of amphiphile to metal ion ratio (1:0.1 to 1:0.3 for Fe 3+ -containing gel and 1:0.25 to 1:0.75 for Hg 2+ -containing gel). The metallo-hydrogels were characterized by different spectroscopic and microscopic techniques, low- and wide-angle powder X-ray diffraction, and small-angle X-ray scattering studies. FT-IR and NMR spectroscopic studies indicate the participation of the imidazole ring in metal-ion binding. Low- and wide-angle powder X-ray diffraction and small-angle X-ray scattering data are in favor of a layered structure of the supramolecular assembly of the AM1 in the presence of metal-ions. Both, the amphiphiles and the metal ion induced hydrogels reveal catalytic activity of p -nitrophenyl esters hydrolysis for the acetyl, n -butyl and n -octyl esters . Ferric ion containing metallo-hydrogel exhibits higher catalytic activity than the corresponding AM1 aggregate in the absence of metal ions.
Keyphrases
- high resolution
- hyaluronic acid
- drug delivery
- wound healing
- aqueous solution
- tissue engineering
- quantum dots
- amino acid
- dual energy
- drug release
- extracellular matrix
- molecular docking
- water soluble
- mass spectrometry
- electron microscopy
- machine learning
- gene expression
- fatty acid
- big data
- endothelial cells
- artificial intelligence
- highly efficient
- diabetic rats
- high glucose
- case control
- data analysis
- binding protein