Shuang Wang, Kaiyu Dong, Dingming Liang, Yunjing Zhang, Xue Li, Tao Song
{"title":"MIPPIS:多信息融合的蛋白质-蛋白质相互作用位点预测网络。","authors":"Shuang Wang, Kaiyu Dong, Dingming Liang, Yunjing Zhang, Xue Li, Tao Song","doi":"10.1186/s12859-024-05964-7","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>The prediction of protein-protein interaction sites plays a crucial role in biochemical processes. Investigating the interaction between viruses and receptor proteins through biological techniques aids in understanding disease mechanisms and guides the development of corresponding drugs. While various methods have been proposed in the past, they often suffer from drawbacks such as long processing times, high costs, and low accuracy.</p><p><strong>Results: </strong>Addressing these challenges, we propose a novel protein-protein interaction site prediction network based on multi-information fusion. In our approach, the initial amino acid features are depicted by the position-specific scoring matrix, hidden Markov model, dictionary of protein secondary structure, and one-hot encoding. Simultaneously, we adopt a multi-channel approach to extract deep-level amino acids features from different perspectives. The graph convolutional network channel effectively extracts spatial structural information. The bidirectional long short-term memory channel treats the amino acid sequence as natural language, capturing the protein's primary structure information. The ProtT5 protein large language model channel outputs a more comprehensive amino acid embedding representation, providing a robust complement to the two aforementioned channels. Finally, the obtained amino acid features are fed into the prediction layer for the final prediction.</p><p><strong>Conclusion: </strong>Compared with six protein structure-based methods and six protein sequence-based methods, our model achieves optimal performance across evaluation metrics, including accuracy, precision, F<sub>1</sub>, Matthews correlation coefficient, and area under the precision recall curve, which demonstrates the superiority of our model.</p>","PeriodicalId":8958,"journal":{"name":"BMC Bioinformatics","volume":"25 1","pages":"345"},"PeriodicalIF":2.9000,"publicationDate":"2024-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11536593/pdf/","citationCount":"0","resultStr":"{\"title\":\"MIPPIS: protein-protein interaction site prediction network with multi-information fusion.\",\"authors\":\"Shuang Wang, Kaiyu Dong, Dingming Liang, Yunjing Zhang, Xue Li, Tao Song\",\"doi\":\"10.1186/s12859-024-05964-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Background: </strong>The prediction of protein-protein interaction sites plays a crucial role in biochemical processes. Investigating the interaction between viruses and receptor proteins through biological techniques aids in understanding disease mechanisms and guides the development of corresponding drugs. While various methods have been proposed in the past, they often suffer from drawbacks such as long processing times, high costs, and low accuracy.</p><p><strong>Results: </strong>Addressing these challenges, we propose a novel protein-protein interaction site prediction network based on multi-information fusion. In our approach, the initial amino acid features are depicted by the position-specific scoring matrix, hidden Markov model, dictionary of protein secondary structure, and one-hot encoding. Simultaneously, we adopt a multi-channel approach to extract deep-level amino acids features from different perspectives. The graph convolutional network channel effectively extracts spatial structural information. The bidirectional long short-term memory channel treats the amino acid sequence as natural language, capturing the protein's primary structure information. The ProtT5 protein large language model channel outputs a more comprehensive amino acid embedding representation, providing a robust complement to the two aforementioned channels. Finally, the obtained amino acid features are fed into the prediction layer for the final prediction.</p><p><strong>Conclusion: </strong>Compared with six protein structure-based methods and six protein sequence-based methods, our model achieves optimal performance across evaluation metrics, including accuracy, precision, F<sub>1</sub>, Matthews correlation coefficient, and area under the precision recall curve, which demonstrates the superiority of our model.</p>\",\"PeriodicalId\":8958,\"journal\":{\"name\":\"BMC Bioinformatics\",\"volume\":\"25 1\",\"pages\":\"345\"},\"PeriodicalIF\":2.9000,\"publicationDate\":\"2024-11-04\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11536593/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"BMC Bioinformatics\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1186/s12859-024-05964-7\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"BMC Bioinformatics","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1186/s12859-024-05964-7","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
MIPPIS: protein-protein interaction site prediction network with multi-information fusion.
Background: The prediction of protein-protein interaction sites plays a crucial role in biochemical processes. Investigating the interaction between viruses and receptor proteins through biological techniques aids in understanding disease mechanisms and guides the development of corresponding drugs. While various methods have been proposed in the past, they often suffer from drawbacks such as long processing times, high costs, and low accuracy.
Results: Addressing these challenges, we propose a novel protein-protein interaction site prediction network based on multi-information fusion. In our approach, the initial amino acid features are depicted by the position-specific scoring matrix, hidden Markov model, dictionary of protein secondary structure, and one-hot encoding. Simultaneously, we adopt a multi-channel approach to extract deep-level amino acids features from different perspectives. The graph convolutional network channel effectively extracts spatial structural information. The bidirectional long short-term memory channel treats the amino acid sequence as natural language, capturing the protein's primary structure information. The ProtT5 protein large language model channel outputs a more comprehensive amino acid embedding representation, providing a robust complement to the two aforementioned channels. Finally, the obtained amino acid features are fed into the prediction layer for the final prediction.
Conclusion: Compared with six protein structure-based methods and six protein sequence-based methods, our model achieves optimal performance across evaluation metrics, including accuracy, precision, F1, Matthews correlation coefficient, and area under the precision recall curve, which demonstrates the superiority of our model.
期刊介绍:
BMC Bioinformatics is an open access, peer-reviewed journal that considers articles on all aspects of the development, testing and novel application of computational and statistical methods for the modeling and analysis of all kinds of biological data, as well as other areas of computational biology.
BMC Bioinformatics is part of the BMC series which publishes subject-specific journals focused on the needs of individual research communities across all areas of biology and medicine. We offer an efficient, fair and friendly peer review service, and are committed to publishing all sound science, provided that there is some advance in knowledge presented by the work.