دورية أكاديمية

Supramolecular protein polymers using mini-ferritin Dps as the building block.

التفاصيل البيبلوغرافية
العنوان: Supramolecular protein polymers using mini-ferritin Dps as the building block.
المؤلفون: Pacheco MR; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt., Jacinto JP; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt., Penas D; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt., Calmeiro T; CENIMAT/i3N, Departamento de Ciências dos Materiais, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal., Almeida AV; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt., Colaço M; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt., Fortunato E; CENIMAT/i3N, Departamento de Ciências dos Materiais, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal., Jones NC; ISA, Department of Physics and Astronomy, Aarhus University, Ny Munkegade 120, DK-8000 Aarhus C, Denmark., Hoffmann SV; ISA, Department of Physics and Astronomy, Aarhus University, Ny Munkegade 120, DK-8000 Aarhus C, Denmark., Pereira MMA; Molecular Synthesis Group, LAQV/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal., Tavares P; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt., Pereira AS; Molecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal. masp@fct.unl.pt.
المصدر: Organic & biomolecular chemistry [Org Biomol Chem] 2020 Nov 25; Vol. 18 (45), pp. 9300-9307.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101154995 Publication Model: Print Cited Medium: Internet ISSN: 1477-0539 (Electronic) Linking ISSN: 14770520 NLM ISO Abbreviation: Org Biomol Chem Subsets: PubMed not MEDLINE; MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : Royal Society of Chemistry, c2003-
مستخلص: A missense mutant of a Dps protein (DNA-binding protein from starved cells) from Marinobacter hydrocarbonoclasticus was used as a building block to develop a new supramolecular assembly complex which enhances the iron uptake, a physiological function of this mini-ferritin. The missense mutation was conducted in an exposed and flexible region of the N-terminal, wherein a threonine residue in position 10 was replaced by a cysteine residue (DpsT10C). This step enabled a click chemistry approach to the variant DpsT10C, where a thiol-ene coupling occurs. Two methods and two types of linker were used resulting in two different mini-ferritin supramolecular polymers, which have maintained secondary structure and native iron uptake physiological function. Electrophoretic assays and mass spectrometry were utilized to confirm that both functionalization and coupling reactions occured as predicted. The secondary structure has been investigated by circular dichroism and synchrotron radiation circular dichroism. Size and morphology were obtained by dynamic light scattering, size exclusion chromatography and atomic force microscopy, respectively. The iron uptake of the synthesized protein polymers was confirmed by UV-Vis spectroscopy loading assays.
تواريخ الأحداث: Date Created: 20201110 Date Completed: 20220310 Latest Revision: 20220310
رمز التحديث: 20240628
DOI: 10.1039/d0ob01702g
PMID: 33169764
قاعدة البيانات: MEDLINE
الوصف
تدمد:1477-0539
DOI:10.1039/d0ob01702g