Publication: Ibitter‐fuse: A novel sequence‐based bitter peptide predictor by fusing multi‐view features
Issued Date
2021-08-02
Resource Type
ISSN
14220067
16616596
16616596
Other identifier(s)
2-s2.0-85112748133
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Mahidol University
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SCOPUS
Bibliographic Citation
International Journal of Molecular Sciences. Vol.22, No.16 (2021)
Suggested Citation
Phasit Charoenkwan, Chanin Nantasenamat, Md Mehedi Hasan, Mohammad Ali Moni, Pietro Lio, Watshara Shoombuatong Ibitter‐fuse: A novel sequence‐based bitter peptide predictor by fusing multi‐view features. International Journal of Molecular Sciences. Vol.22, No.16 (2021). doi:10.3390/ijms22168958 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/76070
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Title
Ibitter‐fuse: A novel sequence‐based bitter peptide predictor by fusing multi‐view features
Abstract
Accurate identification of bitter peptides is of great importance for better understanding their biochemical and biophysical properties. To date, machine learning‐based methods have be-come effective approaches for providing a good avenue for identifying potential bitter peptides from large‐scale protein datasets. Although few machine learning‐based predictors have been developed for identifying the bitterness of peptides, their prediction performances could be improved. In this study, we developed a new predictor (named iBitter‐Fuse) for achieving more accurate identification of bitter peptides. In the proposed iBitter‐Fuse, we have integrated a variety of feature encoding schemes for providing sufficient information from different aspects, namely consisting of compositional information and physicochemical properties. To enhance the predictive perfor-mance, the customized genetic algorithm utilizing self‐assessment‐report (GA‐SAR) was employed for identifying informative features followed by inputting optimal ones into a support vector machine (SVM)‐based classifier for developing the final model (iBitter‐Fuse). Benchmarking experi-ments based on both 10‐fold cross‐validation and independent tests indicated that the iBitter‐Fuse was able to achieve more accurate performance as compared to state‐of‐the‐art methods. To facili-tate the high‐throughput identification of bitter peptides, the iBitter‐Fuse web server was established and made freely available online. It is anticipated that the iBitter‐Fuse will be a useful tool for aiding the discovery and de novo design of bitter peptides.