Peptidylprolyl Isomerase (PPIase): A Promising Drug Target and Biomarker

Target Name: Peptidylprolyl Isomerase

NCBI ID: P14126

Other Name(s): PPIase | Cyclophilin | Peptidylprolyl isomerase

Peptidylprolyl Isomerase (PPIase): A Promising Drug Target and Biomarker

Introduction

Peptidylprolyl isomerase (PPIase) is an enzyme involved in the regulation of protein structure and stability. It is a protein that catalyzes the conversion of proline (P1) to alpha-helix (A1) and alpha-sheet (A2) conformations. PPIase is critical for the regulation of various cellular processes, including cell growth, differentiation, and stress response. The dysfunction of PPIase has been implicated in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. As a result, targeting PPIase has emerged as a promising strategy for the development of new therapeutic approaches.

Drug Targets and Biomarkers

The identification of PPIase as a drug target is based on several factors. Firstly, PPIase has been shown to play a role in various cellular processes that are associated with the development and progression of diseases. For example, altered levels of PPIase have been observed in various cancer types, including breast, ovarian, and prostate cancers. Additionally, increased PPIase activity has been linked to the development of neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases.

Secondly, several small molecules have been shown to inhibit PPIase, leading to the potential for these compounds to act as drug candidates. These molecules have been shown to alter the activity of PPIase, leading to changes in protein structure and function. PPIase inhibitors have been shown to inhibit the growth and survival of cancer cells, as well as to reduce neurodegeneration in neurodegenerative diseases.

Thirdly, the lack of specific inhibitors for PPIase makes it a potential target for drug development. The development of new inhibitors of PPIase can provide a new mechanism of treatment for diseases associated with the dysfunction of PPIase.

Discovery of New Treatments

The development of new treatments for PPIase-related diseases is an active area of 鈥嬧?媟esearch. inhibitors of PPIase have been shown to be effective in preclinical studies for the treatment of various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

For example, a small molecule inhibitor, N-[1-(3-isothiocyanatopyrrolidin-1-yl)-4-piperidinyl]-2,4-dinitrophenyl-1-amine (NIPA), has been shown to inhibit the growth of cancer cells in a variety of formats, including cell lines and animal models. NIPA has also been shown to reduce neurodegeneration in animal models of neurodegenerative diseases, including Alzheimer's and Parkinson's diseases.

Another small molecule inhibitor, 2-fluoro-4-methoxy-7-nitro-2-furanone (FMN), has been shown to inhibit the activity of PPIase and reduce neurodegeneration in animal models of neurodegenerative diseases.

Conclusion

In conclusion, PPIase is a protein involved in the regulation of protein structure and stability that has been implicated in various diseases. The identification of PPIase as a drug target and biomarker has led to the development of new therapeutic approaches for the treatment of PPIase-related diseases. The development of inhibitors of PPIase has the potential to provide new mechanisms of treatment for a variety of diseases. Further research is needed to fully understand the role of PPIase in disease and to develop effective treatments.

Protein Name: Peptidylprolyl Isomerase (nonspecified Subtype)

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