Saliva proteins with important functions for our innate immune system

This proposal seeks beamtime at ESRF BM29 to advance our investigation into the conformational ensemble (CoE) and oligomerization behavior of intrinsically disordered proteins (IDPs), focusing on the salivary peptide Histatin 1 (Hst1). Building on prior work using SAXS and molecular dynamics (MD) simulations of Histatin 5, we now aim to apply similar approaches to the self-associating Hst1 peptide. Our goal is to characterize its oligomeric states using SEC-SAXS under varying concentrations and flow rates, complemented by standard solution measurements. The results will be integrated with explicit water MD simulations to develop a decomposition method for analyzing oligomeric IDP solutions. Given the antiviral potential of Hst1, these studies not only offer structural insights but may also inform future therapeutic applications. We request 48 hours of beamtime to perform SEC-SAXS and BioRobot measurements on ~200 samples, to support this multidisciplinary investigation.