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Spectroscopic Quantification of Plasma Free Hemoglobin Based on Paired Domain Adaptation and Orthogonality Constraints
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DOI：10.1002/jbio.70266.png)
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Abstract
En 中文
Objective We propose a paired domain-adaptation deep regression method for multi-pathlength spectroscopy to quantify plasma free hemoglobin (FHB) robustly across measurement conditions.Methods UV-Vis-NIR spectra (300-1160 nm; 945 wavelengths) were acquired using an Avantes spectrometer, with five optical pathlengths per sample. Spectra were preprocessed by standard normal variate (SNV), and labels were log-transformed (log (1 + y)) to mitigate long-tailed instability. The network integrates domain-path affine calibration, a 1D-CNN encoder, and attention-based multi-path fusion, followed by shared-private feature disentanglement. A paired consistency loss aligns only the shared representation across paired domains, and an orthogonality constraint encourages domain-specific separation. Performance was evaluated via regression-stratified five-fold cross-validation using RMSE and R2 on the raw scale.Results For N = 251 samples, lambda pair = 1.0 achieved RMSE = 260.53 +/- 62.01 and R2 = 0.748 +/- 0.088.Conclusion The method improves cross-domain robustness and interpretability for plasma FHB prediction.
Keywords:
domain adaptation
free hemoglobin
multi-pathlength
plasma
spectroscopy
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