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Active Semisupervised Model for Improving the Identification of Anticancer Peptides

[Image: see text] Cancer is one of the most dangerous threats to human health. Accurate identification of anticancer peptides (ACPs) is valuable for the development and design of new anticancer agents. However, most machine-learning algorithms have limited ability to identify ACPs, and their accurac...

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Detalles Bibliográficos
Autores principales: Cai, Lijun, Wang, Li, Fu, Xiangzheng, Zeng, Xiangxiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8459422/
https://www.ncbi.nlm.nih.gov/pubmed/34568678
http://dx.doi.org/10.1021/acsomega.1c03132
Descripción
Sumario:[Image: see text] Cancer is one of the most dangerous threats to human health. Accurate identification of anticancer peptides (ACPs) is valuable for the development and design of new anticancer agents. However, most machine-learning algorithms have limited ability to identify ACPs, and their accuracy is sensitive to the amount of label data. In this paper, we construct a new technology that combines active learning (AL) and label propagation (LP) algorithm to solve this problem, called (ACP-ALPM). First, we develop an efficient feature representation method based on various descriptor information and coding information of the peptide sequence. Then, an AL strategy is used to filter out the most informative data for model training, and a more powerful LP classifier is cast through continuous iterations. Finally, we evaluate the performance of ACP-ALPM and compare it with that of some of the state-of-the-art and classic methods; experimental results show that our method is significantly superior to them. In addition, through the experimental comparison of random selection and AL on three public data sets, it is proved that the AL strategy is more effective. Notably, a visualization experiment further verified that AL can utilize unlabeled data to improve the performance of the model. We hope that our method can be extended to other types of peptides and provide more inspiration for other similar work.