iAMP-CA2L: a new CNN-BiLSTM-SVM classifier based on cellular automata image for identifying antimicrobial peptides and their functional types.

Predicting antimicrobial peptides (AMPs') function is an important and difficult problem, particularly when AMPs have many multiplex functions, i.e. some AMPs simultaneously have two or three functional classes. By introducing the 'CNN-BiLSTM-SVM classifier' and 'cellular automata image', a new predictor, called iAMP-CA2L, has been developed that can be used to deal with the systems containing both monofunctional and multifunctional AMPs. iAMP-CA2L is a 2-level predictor. The 1st level is to identify whether a given query peptide is an AMP or a non-AMP, while the 2nd level is to predict if it belongs to one or more functional types. As demonstration, the jackknife cross-validation was performed with iAMP-CA2L on a benchmark dataset of AMPs classified into the following 10 functional classes: (1) antibacterial peptides, (2) antiviral peptides, (3) antifungal peptides, (4) antibiofilm peptides, (5) antiparasital peptides, (6) anti-HIV peptides, (7) anticancer (antitumor) peptides, (8) chemotactic peptides, (9) anti-MRSA peptides and (10) antiendotoxin peptides, where none of AMPs included has ≥90% pairwise sequence identity to any other in the same subset. Experiments show that iAMP-CA2L has greatly improved the prediction performance compared with the existing predictors. iAMP-CA2L is freely accessible to the public at the web site http://www.jci-bioinfo.cn/ iAMP-CA2L, and the predictor program has been uploaded to https://github.com/liujin66/iAMP-CA2L.

Using Cellular Automata to Simulate Domain Evolution in Proteins.

Proteins play primary roles in important biological processes such as catalysis, physiological functions, and immune system functions. Thus, the research on how proteins evolved has been a nuclear question in the field of evolutionary biology. General models of protein evolution help to determine the baseline expectations for evolution of sequences, and these models have been extensively useful in sequence analysis as well as for the computer simulation of artificial sequence data sets. We have developed a new method of simulating multi-domain protein evolution, including fusions of domains, insertion, and deletion. It has been observed via the simulation test that the success rates achieved by the proposed predictor are remarkably high. For the convenience of the most experimental scientists, a user-friendly web server has been established at http://jci-bioinfo.cn/domainevo, by which users can easily get their desired results without having to go through the detailed mathematics. Through the simulation results of this website, users can predict the evolution trend of the protein domain architecture.