Parathyroid hormone is the most important endocrine regulator of calcium concentration. Its N-terminal fragment (1-34) has sufficient activity for biological function. Recently, site-directed mutagenesis studies demonstrated that substitutions at several positions within shorter analogues (1-14) can enhance the bioactivity to greater than that of PTH (1-34). However, designing the optimal sequence combination is not simple due to complex combinatorial problems. In this study, support vector machines were introduced to predict the biological activity of modified PTH (1-14) analogues using mono-substituted experimental data and to analyze the key physicochemical properties at each position that correlated with bioactivity. This systematic approach can reduce the time and effort needed to obtain desirable molecules by bench experiments and provide useful information in the design of simpler activating molecules.
Bibliographical noteFunding Information:
This work was supported by the Korea Science and Engineering Foundation grant (to W.L) funded by the Korea government (Ministry of Science and Technology) (R01-2007-000-10161-0). This work was also supported in part by the Brain Korea 21 program.
- Parathyroid hormone
- Peptide analogue
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology