Conformational changes and location of BSA upon immobilization on zeolitic imidazolate frameworks

The location and the conformational changes of proteins/enzymes immobilized within Metal Organic Frameworks (MOFs) are still poorly investigated and understood. Bovine serum albumin (BSA), used as a model protein, was immobilized within two different zeolitic imidazolate frameworks (ZIF-zni and ZIF-8). Pristine ZIFs and BSA@ZIFs were characterized by X-ray diffraction, small-angle X-ray scattering, scanning electron microscopy, confocal laser scanning microscopy, thermogravimetric analysis, micro-FTIR and confocal Raman spectroscopy to characterize MOFs structure and the protein location in the materials. Moreover, the secondary structure and conformation changes of BSA after immobilization on both ZIFs were studied with FTIR. BSA is located both in the inner and on the outer surface of MOFs, forming domains that span from the micro-to the nanoscale. BSA crystallinity (b-sheets + a-heli ces) increases up to 25 % and 40 % due to immobilization within ZIF-zni and ZIF-8, respectively, with a consequent reduction of b-turns.(c) 2023 Elsevier Inc. All rights reserved.

Automated summary

In this study, the location and conformational changes of proteins in Metal Organic Frameworks (MOFs) were investigated. Bovine serum albumin (BSA) was immobilized in two different zeolitic imidazolate frameworks (ZIF-zni and ZIF-8), forming micro-to nanoscale domains. The secondary structure of BSA also changed, with an increase in β-sheets and α-helices and a decrease in β-turns.