Optical Spectroscopic and Morphological Characterizations of Curcuminized Silk Biomaterials: A Perspective from Drug Stabilization.

Silk protein fibroins have gained remarkable attention in recent years as a potential drug carrier in the developing medicinal field of research. In this work, the stability of anticancer agent curcumin in the presence of two different silk protein fibroins from nonmulberry (Am) and mulberry (Bm) has been examined, and the possible mechanism of stabilization in a physiologically relevant medium has also been explored. In solution phase, upon treatment with curcumin, the predominated β-sheet structure of Am is marginally altered, whereas in the case of Bm, a substantial structural changeover has been observed (from coil to β-sheet) to accommodate the hydrophobic drug. Also, the morphological assessments suggest that curcumin is nicely housed in the nanoscaffold of silk fibroin (SF). Consequently, the extent of degradation of curcumin is remarkably suppressed upon encapsulation with the SF. The dissimilarity in the binding patterns of curcumin with these silk proteins could be responsible for the observed difference in the stability orders. Curcumin binds the surface of Bm, whereas in Am, the drug is incorporated in the hydrophobic cavity, and as a consequence, the drug is effectively sequestered out of the aqueous medium. The increase in the fluorescence quantum yield upon interaction with the protein greatly modulates the excited-state intermolecular hydrogen atom transfer (ESIPT) process, which is in tune with a substantial increase in the lifetime of the excited-state of curcumin. The ESIPT is known to play a crucial role in the degradation of curcumin under physiological pH conditions, which perhaps implies its potential therapeutic activity in the presence of silk. The in-depth spectroscopic analyses of curcumin-SF complexes in aqueous medium can provide useful insights for further applicative developments in bioengineering.