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It is challenging to balance high biocompability with good mechanical-electrical sensing performance, especially when triggered inflammatory stress response after in-vivo implantation. Herein, we reported a bioinspired wrinkle-reinforced adaptive nanoclay-interlocked soft strain-sensor based on a highly stretchable and elastic ionic-conductive hydrogel. This novel nanoclay-composite hydrogel exhibited excellent tensile properties and high sensing capacity with steady and reliable sensing performance due to the structural-mechanical-electrical integrity of the nanoclay crosslinked and nano-reinforced interpenetrating network. The incorporation of amphiphilic ions provides the hydrogel with significant protein resistance, reducing its non-specific adsorption to proteins upon implantation and improving its biosafety as an implanted device and maintaining the authenticity of the sensing results. Based on the revealed sensing enhanced mechanism based on hierarchical ordered structures, as a proof-of-concept application, it is for the first time to demonstrate this hydrogel sensor can accurately localize the region where myocardial infarction occurs and may become a novel strategy for real-time monitoring of pathological changes in heart disease. This article is protected by copyright. All rights reserved.

The type I pepsin-soluble collagen (type I PSC) from the red drum fish (Sciaenops ocellatus) scales was successfully purified by hydrophilic ultrafiltration (UF). The collagen purification process was appraised in depth and described in detail, respectively. Based on SDS-PAGE analysis, using proteomics analysis and Isoform-sequencing (Iso-Seq), it was confirmed to be the type I PSC, containing collagen α1 and α2 chains as the single components, with the absence of the non- collagenous proteins, non-type I collagens and potentially allergenic proteins. The type I PSC was verified to be non-denatured collagen monomers with integrated triple-helical structure using gel filtration chromatography (GFC), ion-exchange chromatography (IEC), reversed-phase HPLC (RP-HPLC), fourier transform infrared spectroscopy (FTIR), matrix-assisted laser desorption ionization-time of flight/mass spectrometry (MALDI-TOF/MS) and amino acid composition analysis. Thus, the accurate primary structures of the type I PSC with 100% matched peptide coverage were obtained for the first time. Additionally, our current study is the first to illustrate the protein component changes in collagen induced by hydrophilic UF and the primary structure changes in collagen molecules induced by pepsin solubilization.