**7. Conclusion**

Protein misfolding is the cause of many diseases, and new discoveries about protein misfolding have led to the study of another aspect of protein misfolding described as self-aggregation or self-activation. Various diagnostic approaches have been used to

detect protein aggregates *in vitro* and in living cells. Traditional methods, dye-binding assays, TEM, CD, and FTIR analysis, have been widely used to monitor amyloid fibril formation *in vitro*. Recently, AFM and dot blot assays using conformation-specific antibodies have been used to characterize physiologically important pro fibrillar protein aggregates. A limitation of diagnostic techniques for dye-binding assays is the inadequate detection of prefibrous oligomers by current dyes. Lack of biomarkers and antibodies in protein aggregate detection prohibits prompt diagnosis of conditions relative to protein misfolding. Therefore, as discussed the main theme in therapeutic approach for misfolding of proteins relies on most effective procedure for early diagnosis and understanding the fundamental mechanisms of protein aggregation. Chaperonerelated therapeutic measures are being explored for treatment of protein misfolding diseases. Also, the ubiquitin protease system and unfolded protein responses are being explored molecularly to achieve new insight into misfolding of proteins.
