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One of its most significant advantages is its ability to reduce inflammation, a key factor in slowing down the healing process
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Lakowicz and Gregorio Weber reported that despite their common location in the interior of the protein matrix and the apparent inaccessibility to solvent, no tryptophan residues were excluded from quenching by oxygen (which is an ideal quencher of the fluorescence of singlet excited states, as every collision with an excited fluorophore results in quenching), indicating that proteins, in general, undergo rapid structural fluctuations on the nanosecond time scale which permit diffusion of oxygen (Lakowicz and Weber, 1973)
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