کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1250143 | 1495979 | 2015 | 6 صفحه PDF | دانلود رایگان |
• 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.
Journal: Vibrational Spectroscopy - Volume 80, September 2015, Pages 30–35