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ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding

BACKGROUND: Antimicrobial resistance is one of our most serious health threats. Antimicrobial peptides (AMPs), effecter molecules of innate immune system, can defend host organisms against microbes and most have shown a lowered likelihood for bacteria to form resistance compared to many conventional...

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Autores principales: Fu, Haoyi, Cao, Zicheng, Li, Mingyuan, Wang, Shunfang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7455913/
https://www.ncbi.nlm.nih.gov/pubmed/32859150
http://dx.doi.org/10.1186/s12864-020-06978-0
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author Fu, Haoyi
Cao, Zicheng
Li, Mingyuan
Wang, Shunfang
author_facet Fu, Haoyi
Cao, Zicheng
Li, Mingyuan
Wang, Shunfang
author_sort Fu, Haoyi
collection PubMed
description BACKGROUND: Antimicrobial resistance is one of our most serious health threats. Antimicrobial peptides (AMPs), effecter molecules of innate immune system, can defend host organisms against microbes and most have shown a lowered likelihood for bacteria to form resistance compared to many conventional drugs. Thus, AMPs are gaining popularity as better substitute to antibiotics. To aid researchers in novel AMPs discovery, we design computational approaches to screen promising candidates. RESULTS: In this work, we design a deep learning model that can learn amino acid embedding patterns, automatically extract sequence features, and fuse heterogeneous information. Results show that the proposed model outperforms state-of-the-art methods on recognition of AMPs. By visualizing data in some layers of the model, we overcome the black-box nature of deep learning, explain the working mechanism of the model, and find some import motifs in sequences. CONCLUSIONS: ACEP model can capture similarity between amino acids, calculate attention scores for different parts of a peptide sequence in order to spot important parts that significantly contribute to final predictions, and automatically fuse a variety of heterogeneous information or features. For high-throughput AMPs recognition, open source software and datasets are made freely available at https://github.com/Fuhaoyi/ACEP.
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spelling pubmed-74559132020-08-31 ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding Fu, Haoyi Cao, Zicheng Li, Mingyuan Wang, Shunfang BMC Genomics Research Article BACKGROUND: Antimicrobial resistance is one of our most serious health threats. Antimicrobial peptides (AMPs), effecter molecules of innate immune system, can defend host organisms against microbes and most have shown a lowered likelihood for bacteria to form resistance compared to many conventional drugs. Thus, AMPs are gaining popularity as better substitute to antibiotics. To aid researchers in novel AMPs discovery, we design computational approaches to screen promising candidates. RESULTS: In this work, we design a deep learning model that can learn amino acid embedding patterns, automatically extract sequence features, and fuse heterogeneous information. Results show that the proposed model outperforms state-of-the-art methods on recognition of AMPs. By visualizing data in some layers of the model, we overcome the black-box nature of deep learning, explain the working mechanism of the model, and find some import motifs in sequences. CONCLUSIONS: ACEP model can capture similarity between amino acids, calculate attention scores for different parts of a peptide sequence in order to spot important parts that significantly contribute to final predictions, and automatically fuse a variety of heterogeneous information or features. For high-throughput AMPs recognition, open source software and datasets are made freely available at https://github.com/Fuhaoyi/ACEP. BioMed Central 2020-08-28 /pmc/articles/PMC7455913/ /pubmed/32859150 http://dx.doi.org/10.1186/s12864-020-06978-0 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research Article
Fu, Haoyi
Cao, Zicheng
Li, Mingyuan
Wang, Shunfang
ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
title ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
title_full ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
title_fullStr ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
title_full_unstemmed ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
title_short ACEP: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
title_sort acep: improving antimicrobial peptides recognition through automatic feature fusion and amino acid embedding
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7455913/
https://www.ncbi.nlm.nih.gov/pubmed/32859150
http://dx.doi.org/10.1186/s12864-020-06978-0
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