Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water DOI
Myung Kook Son, Dongjoon Im, Da Gyeong Hyun

et al.

The Journal of Physical Chemistry Letters, Journal Year: 2024, Volume and Issue: unknown, P. 11823 - 11829

Published: Nov. 19, 2024

We explored the influence of D2O on fibrillation kinetics and structural dynamics amyloid intrinsically disordered proteins (IDPs), including α-synuclein, amyloid-β 1–42, K18. Our findings revealed that IDPs was accelerated in compared to H2O, exhibiting faster contrast structured protein, insulin. Structural investigations using electrospray ionization ion mobility mass spectrometry small-angle X-ray scattering combined with molecular simulations demonstrated did not show significant changes could D2O. Umbrella sampling protein protofibrils verified an increased level hydrogen bonding enhanced hydrophobic interactions stabilized β-sheet fibrils These indicate stabilizing a more microenvironment result IDPs. The study highlights importance considering D2O's differential impact when conducting kinetic analyses, particularly for native peptides proteins.

Language: Английский

On the Role of the Glycosylation of Type I Collagen in Bone DOI Creative Commons

Luco Rutten,

Elena Macías‐Sánchez, Nico A. J. M. Sommerdijk

et al.

Journal of Structural Biology, Journal Year: 2024, Volume and Issue: 216(4), P. 108145 - 108145

Published: Oct. 22, 2024

Language: Английский

Citations

1
Mechanism of protofibril formation in aqueous collagen solutions DOI Creative Commons
Л. А. Булавін, K.V. Cherevko, O.V. Khorolskyi

et al.

AIP Advances, Journal Year: 2024, Volume and Issue: 14(11)

Published: Nov. 1, 2024

The shear viscosity of aqueous collagen solutions was experimentally investigated over the temperature range 303–353 K and concentrations 1–7 wt. %. A structural phase transition observed at ∼315 K, corresponding to onset protofibril formation. It is shown that below this temperature, protofibrils containing both ordered disordered segments are formed, with proportion increasing as decreases, reaching ∼30% 303 K. An analysis dependence order parameter for in water–collagen system suggests exhibits characteristics a second-order transition.

Language: Английский

Citations

1
Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water DOI
Myung Kook Son, Dongjoon Im, Da Gyeong Hyun

et al.

The Journal of Physical Chemistry Letters, Journal Year: 2024, Volume and Issue: unknown, P. 11823 - 11829

Published: Nov. 19, 2024

We explored the influence of D2O on fibrillation kinetics and structural dynamics amyloid intrinsically disordered proteins (IDPs), including α-synuclein, amyloid-β 1–42, K18. Our findings revealed that IDPs was accelerated in compared to H2O, exhibiting faster contrast structured protein, insulin. Structural investigations using electrospray ionization ion mobility mass spectrometry small-angle X-ray scattering combined with molecular simulations demonstrated did not show significant changes could D2O. Umbrella sampling protein protofibrils verified an increased level hydrogen bonding enhanced hydrophobic interactions stabilized β-sheet fibrils These indicate stabilizing a more microenvironment result IDPs. The study highlights importance considering D2O's differential impact when conducting kinetic analyses, particularly for native peptides proteins.

Language: Английский

Citations

0