Metal-Organic Frameworks with Enzyme-Inspired Catalytic Activity

A. M. FRACAROLI; R. H. DE ROSSI; O. M. YAGHI

Concón

Conferencia; 14th Latin American Conference on Physical Organic Chemistry (CLAFQO-14); 2017

Pontificia Universidad Católica de Chile

Metal-organic frameworks (MOFs) are an extensive class of crystalline porous materials that show promise in several fields due to their adjustable chemical functionality, structural diversity, and ease of functionalization1.To achieve enzyme-like complexity within the pores of a MOF, it is neccesary to perform multiple covalent-bond-formation reactions on the MOF crystals without losing access to its interior nor cristallinity. Here, we show that seven postsynthetic reactions can be successfully achieved in tandem within the pores of a multivariate MOF, MTV-IRMOF-74-III, to covalently incorporate tripeptides that resemble the active sites of enzymes in their spatial arrangement and compositional heterogeneity.These reactions build up H2N-Pro-Gly-Ala-CONHL and H2N-Cys-His-AspCONHL (where L = organic struts) amino acid sequences by covalently attaching them to the organic struts in the MOFs, without losing porosity or crystallinity. An enabling feature of this chemistry is that the primary amine functionality (−CH2NHBoc) of the original MOF is more reactive than the commonly examined aromatic amines (−NH2), and this allowed for the multi-step reactions to be carried out in tandem within the MOF. Preliminary findings indicate that the complexity thus achieved can affect reactions that were previously accomplished only in the presence of enzymes.