Particle size and morphology-selective synthesis of mesoporous silica and study of its interaction with human serum albumin: spherical versus rod-like shape

Mesoporous silica (MS) has gained considerable attention as a promising material for biomedical applications. The morphology of MS can affect its interaction with biomacromolecules, leading to changes in their biological performance. Herein, we aim to study human serum albumin (HSA) binding to spherical MS (SMS) versus rod-like MS (RMS). For this purpose, the Stober method is exploited and the impact of synthesis variables on the MS morphology and size is examined. Next, the binding of SMS versus RMS with HSA is evaluated using fluorescence spectroscopy. The intrinsic fluorescence intensity changes show the combined dynamic and static quenching mechanism with the dominant contribution of the static mode in the MSs interaction with HSA. However, the RMS-HSA complex is more stable, with a binding constant of 0.03 x 10(6) M-1 at 37 degree celsius compared to the SMS-HAS complex. The hydrophobic interaction is the driving force for SMS and RMS binding to HSA.