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.

Ibitter‐fuse: A novel sequence‐based bitter peptide predictor by fusing multi‐view features / Charoenkwan, P.; Nantasenamat, C.; Hasan, M. M.; Moni, M. A.; Lio, P.; Shoombuatong, W.. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1422-0067. - 22:16(2021). [10.3390/ijms22168958]

Ibitter‐fuse: A novel sequence‐based bitter peptide predictor by fusing multi‐view features

Lio P.;
2021

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.
2021
Bioinformatics; Bitter peptide; Classification; Feature selection; Machine learning; Support vector machine
01 Pubblicazione su rivista::01a Articolo in rivista
Ibitter‐fuse: A novel sequence‐based bitter peptide predictor by fusing multi‐view features / Charoenkwan, P.; Nantasenamat, C.; Hasan, M. M.; Moni, M. A.; Lio, P.; Shoombuatong, W.. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1422-0067. - 22:16(2021). [10.3390/ijms22168958]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1723818
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