Nature Search

Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain

This study identifies potential aggregation hotspots on the fibril surface of Alzheimer’s disease associated Aβ42 fibrils, which are blocked by the anti-amyloid chaperone-like domain BRICHOS.

Rakesh Kumar
Tanguy Le Marchand
Axel Abelein
ResearchOpen Access01 Feb 2024
Nature Communications

Volume: 15, P: 1-10
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

Recombinant spider silks are of interest but the multimodal and aggregation-prone nature of them is a limitation. Here, the authors report on a miniature spidroin based on the N-terminal domain which forms a hydrogel at 37 °C which allows for ease of production and fusion protein modification to generate functional biomaterials.

Tina Arndt
Kristaps Jaudzems
Anna Rising
ResearchOpen Access15 Aug 2022
Nature Communications

Volume: 13, P: 1-14
Halogen-bonded shape memory polymers

Halogen bonding is widely adopted in organic synthesis and supramolecular crystal engineering but application of halogen bonding in the design of stimuli-responsive materials is challenging. Here, the authors report a liquid crystalline network that contains dynamic halogen-bond crosslinks and possesses reversible thermo-responsive shape memory behaviour.

Hongshuang Guo
Rakesh Puttreddy
Arri Priimagi
ResearchOpen Access05 Dec 2022
Nature Communications

Volume: 13, P: 1-10
Efficient protein production inspired by how spiders make silk

The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.

Nina Kronqvist
Médoune Sarr
Jan Johansson
ResearchOpen Access23 May 2017
Nature Communications

Volume: 8, P: 1-15
Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

The molecular mechanism by which rapid spider silk assembly occurs in the glands of spiders is challenging to investigate. Here, the authors perform site-directed mutagenesis of the N-terminal domain and propose a three-step mechanism that allows controlled aggregation of spidroins.

Nina Kronqvist
Martins Otikovs
Jan Johansson
Research10 Feb 2014
Nature Communications

Volume: 5, P: 1-11
Structural basis of epitope recognition by anti-alpha-synuclein antibodies MJFR14-6-4-2

Ilva Liekniņa
Lasse Reimer
Kaspars Tārs
ResearchOpen Access27 Oct 2024
npj Parkinson's Disease

Volume: 10, P: 1-14
Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis

A method for cell-free synthesis of amyloid fibrils is reported that also allows for solid-state NMR analysis to characterize complex and pathological fibrillary assemblies.

Alons Lends
Asen Daskalov
Antoine Loquet
ResearchOpen Access09 Nov 2022
Communications Biology

Volume: 5, P: 1-10
Fused isoselenazolium salts suppress breast cancer cell growth by dramatic increase in pyruvate-dependent mitochondrial ROS production

Marina Makrecka-Kuka
Pavels Dimitrijevs
Pavel Arsenyan
ResearchOpen Access09 Dec 2020
Scientific Reports

Volume: 10, P: 1-12
High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

Axel Abelein
Gefei Chen
Henrik Biverstål
ResearchOpen Access14 Jan 2020
Scientific Reports

Volume: 10, P: 1-10

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