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Tytuł pozycji:

Macromolecular and Solution Properties of the Recombinant Fusion Protein HUG.

Tytuł:
Macromolecular and Solution Properties of the Recombinant Fusion Protein HUG.
Autorzy:
Sist P; Department of Life Sciences, University of Trieste, Via Giorgieri 1, Trieste I-34127, Italy.
Bandiera A; Department of Life Sciences, University of Trieste, Via Giorgieri 1, Trieste I-34127, Italy.
Urbani R; Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via Giorgieri 1, Trieste I-34127, Italy.
Passamonti S; Department of Life Sciences, University of Trieste, Via Giorgieri 1, Trieste I-34127, Italy.
Źródło:
Biomacromolecules [Biomacromolecules] 2022 Aug 08; Vol. 23 (8), pp. 3336-3348. Date of Electronic Publication: 2022 Jul 25.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Original Publication: Washington, DC : American Chemical Society, c2000-
MeSH Terms:
Bilirubin*
Elastin*/chemistry
Elastin*/genetics
Fluorescence ; Humans ; Peptides/chemistry ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics
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Substance Nomenclature:
0 (Peptides)
0 (Recombinant Fusion Proteins)
9007-58-3 (Elastin)
RFM9X3LJ49 (Bilirubin)
Entry Date(s):
Date Created: 20220725 Date Completed: 20220809 Latest Revision: 20220812
Update Code:
20240105
PubMed Central ID:
PMC9364316
DOI:
10.1021/acs.biomac.2c00447
PMID:
35876275
Czasopismo naukowe
The recombinant fusion protein HELP-UnaG (HUG) is a bifunctional product that exhibits human elastin-like polypeptide (HELP)-specific thermal behavior, defined as a reverse phase transition, and UnaG-specific bilirubin-dependent fluorescence emission. HUG provides an interesting model to understand how its two domains influence each other's properties. Turbidimetric, calorimetric, and light scattering measurements were used to determine different parameters for the reverse temperature transition and coacervation behavior. This shows that the UnaG domain has a measurable but limited effect on the thermal properties of HELP. Although the HELP domain decreased the affinity of UnaG for bilirubin, HUG retained the property of displacing bilirubin from bovine serum albumin and thus remains one of the strongest bilirubin-binding proteins known to date. These data demonstrate that HELP can be used to create new bifunctional fusion products that pave the way for expanded technological applications.

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