ArticleBiophotonics discovery2026
Temperature-induced hemoglobin dynamics: oxygenation-dependent evolution of hemoglobin spectral response in the near-infrared.
Article in Biophotonics discovery, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Significance: Monitoring thermally induced optical changes can guide thermal therapies, but these signals depend strongly on hemoglobin oxygenation, leading to different spectral responses under Aim: We characterized near-infrared absorption spectra of hemoglobin during heating under controlled oxygenated and deoxygenated conditions and related the signatures to hemoglobin chemistry. Approach: Using time-domain diffuse optical spectroscopy, we measured 680- to 1110-nm absorption spectra of blood phantoms containing oxyhemoglobin (oxyHb) or deoxyhemoglobin (deoxyHb) during controlled heating. Multi-concentration measurements yielded extinction coefficients for native and thermally denatured species. Results: Heating oxyHb caused a broad absorption rise consistent with autoxidation of ferrous ( Conclusions: Thermal denaturation of hemoglobin follows distinct oxygenation-dependent spectroscopic pathways. The extracted extinction coefficients provide essential inputs for optical models of laser-based ablation and improve diffuse optical monitoring of thermal therapies.
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