These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Conformational changes and location of BSA upon immobilization on zeolitic imidazolate frameworks.
    Author: Tocco D, Chelazzi D, Mastrangelo R, Casini A, Salis A, Fratini E, Baglioni P.
    Journal: J Colloid Interface Sci; 2023 Jul; 641():685-694. PubMed ID: 36965340.
    Abstract:
    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 (β-sheets + α-helices) increases up to 25 % and 40 % due to immobilization within ZIF-zni and ZIF-8, respectively, with a consequent reduction of β-turns.
    [Abstract] [Full Text] [Related] [New Search]