Self-assembled peptide-based nanobiomaterials exhibit promising prospects for drug delivery applications owing to their commendable biocompatibility and biodegradability, facile tissue uptake and utilization, and minimal or negligible unexpected toxicity. TFF3 is an active peptide autonomously secreted by gastric mucosal cells, possessing multiple biological functions. It acts on the surface of the gastric mucosa, facilitating the repair process of gastric mucosal damage. However, when used as a drug, TFF3 faces significant challenges, including short retention time in the gastric mucosal cavity and deactivation due to degradation by stomach acid. In response to this challenge, we developed a self−assembled short peptide hydrogel, Rqdl10, designed as a delivery vehicle for TFF3. Our investigation encompasses an assessment of its properties, biocompatibility, controlled release of TFF3, and the mechanism underlying the promotion of gastric mucosal injury repair. Congo red/aniline blue staining revealed that Rqdl10 promptly self-assembled in PBS, forming hydrogels. Circular dichroism spectra indicated the presence of a stable β-sheet secondary structure in the Rqdl10 hydrogel. Cryo-scanning electron microscopy and atomic force microscopy observations demonstrated that the Rqdl10 formed vesicle-like structures in the PBS, which were interconnected to construct a three-dimensional nanostructure. Moreover, the Rqdl10 hydrogel exhibited outstanding biocompatibility and could sustainably and slowly release TFF3. The utilization of the Rqdl10 hydrogel as a carrier for TFF3 substantially augmented its proliferative and migratory capabilities, while concurrently bolstering its anti-inflammatory and anti-apoptotic attributes following gastric mucosal injury. Our findings underscore the immense potential of the self-assembled peptide hydrogel Rqdl10 for biomedical applications, promising significant contributions to healthcare science.

Mitochondrial dysfunction, particularly involving energy metabolism, oxidative stress, and structural integrity, is recognized as a critical factor in the pathogenesis of hearing loss. However, evidence regarding a potential association between mitochondrial function and sudden sensorineural hearing loss (SSNHL) remains limited. This study aims to explore the potential causal relationship between mitochondrial biological function and SSNHL using Mendelian randomization (MR) analysis. We utilized genome-wide association study data on SSNHL from the FinnGen database, along with mitochondria-related genome-wide association study summary statistics from previously published studies. Inverse variance weighting served as the primary MR method, using genetic instruments associated with mitochondrial biological function to estimate their effects on SSNHL risk. Sensitivity analyses—including MR-Egger regression, MR-PRESSO, and leave-one-out analysis—were conducted to assess the robustness of the findings and to exclude potential biases. Three mitochondrial proteins were found to exhibit potential causal effects on SSNHL. MUL1 was identified as a potential risk factor, whereas HINT2 and GRPEL1 appeared to serve as potential protective factors. This study provides evidence supporting a potential causal role of mitochondrial biological function in SSNHL. The findings offer novel insights into the mechanistic underpinnings of SSNHL and emphasize the importance of mitochondrial pathways in its pathophysiology. These results may encourage otolaryngologists to consider targeting mitochondrial energy metabolism in the development of more effective clinical prevention and treatment strategies for SSNHL.