**8. Acknowledgment**

644 Biomedical Science, Engineering and Technology

consuming and it is possible for a performer to be exposed to pathogens during the operation. The peptides with a CSαβ motif have been shown to form pores on an artificial membrane, but the artificial membrane does not represent the membrane of different organisms. A new high throughput screening recruiting membrane of different pathogens

Not simple as binding assay, enzymes act on specific substrates and it is extremely difficult to unify experimental conditions for a broad spectrum of enzymes. *In vitro* enzyme inhibitory assays are costly and unable to represent the actually physiological conditions. Computer aided drug screening methods have been established to screen drugs with small molecule weights that can fit into active sites of target proteins (Barrons, 2004;Weideman et al., 1999). Drug dynamics also can be *in silico* simulated (Sinek et al., 2009;Zunino et al., 2009). An antibody can be as a simple binder and its binding targets usually are short fragments exposed to the surface of the proteins. The binding fragments are predicable for a huge amount of knowledge accumulated in the last several decades (Blythe & Flower, 2005;Kulkarni-Kale et al., ;Odorico & Pellequer, 2003). Currently, we do not well understand the interface between peptides with a CSαβ motif and their targets. How functional loops access active sites of the targets is needed to be decrypted. We know too little about the scaffold and it is to difficult to engineer it. It is hard to develop an algorithm to predict the biochemical functions of the peptides with a CSαβ motif. For the complexity of protein-

To biopharma companies, protein engineering/evolution platforms must provide solutions to improve the throughput, safety, biodistribution, activity and frequency of dosing of designed protein, evading intellectual property issues and reducing manufacturing costs, especially in the late process of development and production stages. Intellectual property rights are definite issues, the intellectual property situations of antibodies are obscure as previously described. An alternative scaffold equips the same abilities as antibody does is a valuable prospect and desired to avoid the complex intellectual property landscape of antibody. A protein scaffold can access to a cardinal target and circumvent intellectual property issues that does not mean that it is necessarily a platform worth investing in. The successfully designed protein must equip an improved performance and provide solutions

The knowledge about the scaffold is not enough to establish rules to predict its biochemical functions. There are still some technical limitations and the development of the scaffold is confined. Peptides with a CSαβ motif bear many excellent properties and can serve as an alternative protein scaffold for biomedical application. Natural products containing peptides with a CSαβ motif have been therapeutically used for hundreds of years. Some of the purified peptides are tested and have low toxicities to mammalian species. Prudential is needed when recruiting new proteins/peptides as treatments for diseases. The intellectual property situation of peptides with a CSαβ motif is not as complex as antibody, especially in biomedical application (Yang & Lyu, 2008). For its original expression in plant, the engineered proteins with medicinal effect can be expressed in transgenic crops and diseases

will be a great help in resolving the problem (Yang & Lyu, 2008).

protein interaction, it is a long way to screen peptide drugs *in silico*.

**6. Business issue** 

**7. Conclusion** 

to the concerned points described above.

We sincerely thank Professor Ping-Chiang Lyu at the College of Life Science, National Tsing-Hua University for his kind and generous suggestions. We also thank Dr. Chung-Chang Liu, the senior expert of Industrial Technology Research Institute (ITRI), for his supporting part of the research of this work during his term as the director of Biomedical Engineering Research Laboratories, ITRI.
