Method for identifying the conformational state of proteins
Introduction
A method for the identification and analysis of changes in the conformation and structure of proteins that allows to determine whether they are in the native, denatured or in an aggregated state. This method involves the use of a probe and simple and widely used analysis tools in laboratories, such as UV-Visible spectroscopy and fluorescence microscopy.

Technical features
The method for identifying the conformational states of proteins involves the use of probes, in this specific case a derivative of Bodipy, capable of interacting with proteins in order to identify their conformational states by means of UV-Visible spectroscopy and / or microscopy techniques. in fluorescence. This method also allows to determine the amount of proteins, protein aggregation and fibrillation, amyloid fibrils, amyloid aggregates in fixed histological tissues. The method includes the preparation of a probe stock solution and a working solution. The identification of the conformational state is evident from the formation of protein aggregates clearly evidenced by a clear and marked red fluorescence of the aggregates subjected to fluorescence microscopy.
Possible Applications
- Pharmaceutical industries;
- Cosmetic industries;
- Biotechnological industries;
- Hospitals;
- Research centers.
Advantages
- Increased definition of aggregates;
- Greater sensitivity;
- Applicable, also, to fixed tissues obtained from subjects suffering from amyloid diseases;
- The probe can be used both in UV-Visible spectroscopy and in fluorescence microscopy;
- Increased luminosity and definition of fluorescence fibrils;
- Reduced identification times and costs compared to pre-existing techniques.