Which factors govern the adsorption of peptides to Zr(iv)-based metal–organic frameworks?

Abstract

Fundamental insight into the interactions between biological molecules and materials is essential for the design and development of adsorbents for many applications. Herein, we use a range of peptides to...

Understanding the Role of Surfactants in the Interaction and Hydrolysis of Myoglobin by Zr‐MOF‐808

“…Moreover, these linear hydrophobic tails of SDS and Zw3‐12 are in in contrast with the bulky structure of CHAPS or aromatic nature of TX‐100 which could interact with the aromatic linker of the MOF via π‐π‐ stacking interactions [37] . In addition, the bulky nature of these surfactants may make the micellar structures less stable and easier to disrupt than the linear surfactants, increasing adsorption onto the MOF.…”

MOF catalysis meets biochemistry: molecular insights from the hydrolytic activity of MOFs towards biomolecules

“…In the case of peptides, one of the few systematic studies addressing their adsorption by Zr-MOFs identified many different driving forces for the adsorption to occur. 50 More specifically, the Zr 6 O 8 cluster node has been found to exert a double role by strongly coordinating the carboxylate groups, but also repelling positively charged protonated N-terminal groups. These effects are so important that the distance between C-, and N-terminal ends in a dipeptide was found to affect the extent of adsorption.…”

“…For the MOF-808, UiO-66, and NU-1000 triad, it has been observed that lower connectivity, thus a higher number of available Zr( iv ) sites, correlates with enhanced glycylglycine (Gly-Gly) adsorption. 50 When considering a wide selection of dipeptides, increased hydrophilicity of the peptide's side chain further boosts adsorption in the case of MOF-808. On the other side, the hydrophobicity of H 4 TBAPy , used as the linker for NU-1000, negatively affects the adsorption of Gly-Gly although NU-1000 features very large pores ( cf.…”

“…91 Put into perspective, these findings underline the relevance of tuning the interactions between polar/charged substrates like peptides and linkers for achieving a desired reactivity, in line with the observed for adsorption trends mentioned previously. 50 However, systematic studies on these effects have yet to be reported.…”

CuCoO2 Nanoparticles as a Nanoprotease for Selective Proteolysis with High Efficiency at Room Temperature

“…For example, many nanoproteases, such as metal–organic framework (MOFs), [5] metal‐oxo clusters (MOCs) [6] and metal‐substituted polyoxometalates (POMs) [7] have been reported to selectively cleave proteins to produce medium‐sized fragments, which are the optimal molecular weight range for low and medium proteomics analyses [8] . However, the strong interactions between proteins/peptides and MOCs [6] or MOFs [9] hamper the desorption of products from nanoproteases and result in the low catalyst efficiency and poor recyclability of nanoproteases. Therefore, MOFs, [10] MOCs [11] and POMs [12] usually suffer from the low rate of catalytic hydrolysis with the high proteolytic reaction temperature of 60 °C and long reaction time of 1–8 days [13] .…”