Synchrotron μ-FTIR highlights amyloid-β conformational changes under the effect of surface wettability and external agents

•Integration of nanostructured surfaces in a synchrotron μ-FTIR setup.•Surface roughness influences peptide aggregation at the solid–liquid interface.•Acetylcholinesterase and curcumin affect Aβ secondary structure at early stages.

Here we propose a method to monitor and investigate conformational changes of peptides of high biomedical interest on conventional and nanostructured surfaces by synchrotron infrared micro-spectroscopy. The presence of surfaces with different wettability and the influence of external agents such as acetylcholinesterase and curcumin resulted in marked secondary structure variations of several amyloid-β fragments (namely Aβ(12–28), Aβ(25–35), Aβ(1–40), Aβ(1–42)). The platform could represent a useful tool for the investigation of early stage structural modifications of peptides involved in pathologies of different kind.