Metal-organic frameworks (MOFs) are an intriguing class of hybrid materials that consist of infinite crystalline lattices formed by metal ions bridged by organic linkers. Their porous interiors have highly variable properties, depending on the metal ions and linkers used. To date, MOFs have primarily been examined for uses such as gas separation and storage and catalysis, but recently researchers have described the adsorption of proteins and peptides, such as cytochrome C and a trypsin digest of bovine serum albumin, in MOF pores. The MOF pore provides a stable, ordered environment in which to isolate and characterize peptides. Our research thus far has suggested that MOF-5 readily adsorbs proteins and peptides, however most preparations of MOF-5 suffer from water sensitivity. This is problematic because water or water-based solutions are the most relevant solvent for disease-relevant peptides. We therefore have explored reported methods to improve the hydrostability of MOF-5 through several doping techniques as well as annealing processes. We then studied the adsorption behavior of MOF-5 derivatives toward a number of peptides, the results of which are presented here. Through these studies we strive to understand which differences brought about by structural changes may facilitate selective peptide adsorption.

Modification of MOF-5 hydrostability for peptide adsorption studies

249th National Meeting (2015)

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