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    Home » News » New method detects collagen damage in the skin early, before visible signs appear
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    New method detects collagen damage in the skin early, before visible signs appear

    healthadminBy healthadminJuly 16, 2026No Comments3 Mins Read
    New method detects collagen damage in the skin early, before visible signs appear
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    An international team led by Hiroshima University researchers has developed a new method to detect subtle early changes in collagen in human skin, before any visible signs of damage appear. This study ACS nano July 16, 2026 It has been revealed that the molecular organization and supramolecular chirality, or structural handedness, of dermal collagen breaks down before the visible fiber network actually thins or fragments.

    Collagen is a hierarchical substance that forms a highly organized network that supports the structure and mechanical strength of the skin. Traditional imaging techniques can easily identify visible degradation, such as fiber thinning or loss of connectivity. However, these structural defects represent a later stage of tissue remodeling.

    One way to think about our findings is that while traditional imaging techniques can show the “bricks” of collagen structure, they may miss subtle changes in how those bricks are arranged. This is similar to detecting changes in the arrangement of words and sentences in a book before pages become damaged or missing. ”


    Ali Haider, lead author of the study on knot chiral metamatter and graduate research fellow at the International Institute for Sustainability, Hiroshima University (WPI-SKCM²)

    To uncover these hidden patterns, the team integrated chiroptical spectroscopy with advanced optical imaging, such as synchrotron vacuum ultraviolet circular dichroism (SR-VUVCD) and multidimensional quantum cascade laser vibrational circular dichroism (MultiD-QCL-VCD). This framework allowed us to map both the presence of collagen and its chiral structural consistency in exactly the same physical tissue sections.

    The results demonstrated that collagen mass and structural order are clearly decoupled. Tissue samples retained their bulk collagen content and coverage even after the coherence of their underlying supramolecular chirality was significantly reduced.

    “The key message of this paper is that we should view collagen not only as a visible fibrous network, but also as a hierarchical material whose function depends on organization across multiple length scales,” said Professor Katsuya Inoue of WPI-SKCM², one of the study’s corresponding authors. “Our study shows that advanced correlational techniques can reveal changes in this hidden tissue that are not obvious from morphology alone.”

    The researchers’ goal is to establish a comprehensive framework that integrates molecular chirality, supramolecular organization, and macroscopic organization. This provides insight into medical interventions, wound healing, and biomaterial design, allowing researchers to assess tissue integrity before irreversible macroscopic destruction occurs.

    The research was conducted by Ali Haider, Yusuke Kochi, Andrew K. Schultz, Kuya Aoyama, Aiko Sada, Hisako Sato, Elisabetta Matsumoto, Malcolm Kaddwala, Koichi Matsuo, and Katsuya Inoue. The authors represent an interdisciplinary collaboration between Hiroshima University (including WPI-SKCM², the Graduate School of Advanced Science and Engineering, the Center for Chirality Research, and the Institute for Synchrotron Radiation Science), the Max Planck Institute for Intelligent Systems, Kyushu University, Kumamoto University, Ehime University, Georgia Institute of Technology, and the University of Glasgow. The collaboration spans Japan, Germany, the US and the UK, bringing together expertise from around the world.

    This research was supported by WPI-SKCM², the Henri Poincaré Institute, LabEx CARMIN, and the Alexander von Humboldt Foundation.

    sauce:

    Reference magazines:

    Haider, A. Others. (2026). A correlative multimodal framework reveals a loss of supramolecular chirality that precedes fibrillar thinning of dermal collagen. ACS nano. DOI: 10.1021/acsnano.6c06602. https://pubs.acs.org/doi/10.1021/acsnano.6c06602



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