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Caption : figure s1. standard curve illustrating the correlation between variations in absorbance and the corresponding quantity of tyrosine introduced.

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Caption : figure s2. in situ reflectometric interference spectra showing the immobilizing of casein and the subsequent casein digestion by chymotrypsin. the inset is an enlarged view of the interference peaks with wavelengths between 450 and 500 nm.

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Caption : figure s3 stability of the casein functional layer formed by adsorption: (i) stabilizing the baseline with pbs solution, (ii) functionalization of silica surface with casein, (iii) rinsing with pbs. the change in optical thickness was recorded in real time.

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Caption : figure s4 real-time tracking of alterations in the ot of the scc film following the introduction of the fibrinogen and thrombin mixture into the sample reservoir.

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Caption : figure s5 infrared spectroscopy of fibrin via optical interference. in this spectrum, the amide a band is observed between 3600-3100 cm-1, predominantly arising from n-h stretching vibrations and interactions within the hydrogen-bonding network. the amide i band, indicative of strong absorption, is located in the 1700-1600 cm-1 range, attributed to the c=o stretching vibrations. lastly, the amide ii band, detected between 1580-1500 cm-1, results from the coupling of n-h bending and c-n stretching vibrations.