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AbstractAmidst the contemporary global trends of “hyper-localised” and “sustainable” fashion, the craft-based industries have been given substantial importance in recent times. Realising the competence of the Handloom weaving industry in Sri Lanka within the global fashion industry, this research proposes a new product development approach using the socio-emotional identities of the Handloom artisans. The study takes a practice-led approach following an initial data collection through qualitative research where a purposive sample of twenty-seven Handloom artisans from three provinces in Sri Lanka are interviewed and observed to identify their socio-emotional identities. The study subsequently guides the creation of an un-cut handloom textile developed by the artisans to explore the potential portrayal of the socio-emotional identities of a cross-section of Handloom weavers in Sri Lankan in the final product. This practice-led research chiefly contributes to the Handloom textile sector of Sri Lanka as it provides innovative and unforeseen avenues for new product development and contributes to the existing knowledge of craft-based research. The study affirms the need for acknowledging the Handloom artisans in Sri Lanka and adapting artisan-oriented approaches in future product development. These findings are also valuable in new product development for the Handloom weaving industry in the countries sharing the same industry attributes in the South Asian region.

Amyloid-β (Aβ) fibrils in neuritic plaques are a hallmark of Alzheimer’s disease (AD). Since the 42-residue Aβ (Aβ42) fibril is the most pathogenic among different Aβ species, its structural characterization is crucial to our understanding of AD. While several polymorphs have been reported for Aβ40, previous studies of Aβ42 fibrils prepared at neutral pH detected essentially only one structure, with an S-shaped β-sheet arrangement (e.g., Xiao et al. Nat. Struct. Mol. Biol.2015, 22, 499). Herein, we demonstrate the feasibility of characterizing the structure of trace amounts of brain-derived and synthetic amyloid fibrils by sensitivity-enhanced 1H-detected solid-state NMR (SSNMR) under ultrafast magic angle spinning. By taking advantage of the high sensitivity of this technique, we first demonstrate its applicability for the high-throughput screening of trace amounts of selectively 13C- and 15N-labeled Aβ42 fibril prepared with ∼0.01% patient-derived amyloid (ca. 4 pmol) as a seed. The comparison of 2D 13C/1H SSNMR data revealed marked structural differences between AD-derived Aβ42 (∼40 nmol or ∼200 μg) and synthetic fibrils in less than 10 min, confirming the feasibility of assessing the fibril structure from ∼1 pmol of brain amyloid seed in ∼2.5 h. We also present the first structural characterization of synthetic fully protonatedAβ42 fibril by 1H-detected 3D and 4D SSNMR. With procedures assisted by automated assignments, main-chain resonance assignments were completed for trace amounts (∼42 nmol) of a fully protonatedamyloid fibril in the 1H-detection approach. The results suggest that this Aβ42 fibril exhibits a novel fold or polymorph structure.