Search

Anti-coronavirus peptides (ACVPs) represent a relatively novel approach of inhibiting the adsorption and fusion of the virus with human cells. Several peptide-based inhibitors showed promise as potential therapeutic drug candidates. However, identifying such peptides in laboratory experiments is both costly and time consuming. Therefore, there is growing interest in using computational methods to predict ACVPs. Here, we describe a model for the prediction of ACVPs that is based on the combination of feature engineering (FE) optimization and deep representation learning. FEOpti-ACVP was pre-trained using two feature extraction frameworks. At the next step, several machine learning approaches were tested in to construct the final algorithm. The final version of FEOpti-ACVP outperformed existing methods used for ACVPs prediction and it has the potential to become a valuable tool in ACVP drug design. A user-friendly webserver of FEOpti-ACVP can be accessed at http://servers.aibiochem.net/soft/FEOpti-ACVP/. [ABSTRACT FROM AUTHOR]

Umami peptides enhance the umami taste of food and have good food processing properties, nutritional value, and numerous potential applications. Wet testing for the identification of umami peptides is a time-consuming and expensive process. Here, we report the iUmami-DRLF that uses a logistic regression (LR) method solely based on the deep learning pre-trained neural network feature extraction method, unified representation (UniRep based on multiplicative LSTM), for feature extraction from the peptide sequences. The findings demonstrate that deep learning representation learning significantly enhanced the capability of models in identifying umami peptides and predictive precision solely based on peptide sequence information. The newly validated taste sequences were also used to test the iUmami-DRLF and other predictors, and the result indicates that the iUmami-DRLF has better robustness and accuracy and remains valid at higher probability thresholds. The iUmami-DRLF method can aid further studies on enhancing the umami flavor of food for satisfying the need for an umami-flavored diet. [ABSTRACT FROM AUTHOR]

Summary Identifying the protein–peptide binding residues is fundamentally important to understand the mechanisms of protein functions and explore drug discovery. Although several computational methods have been developed, most of them highly rely on third-party tools or complex data preprocessing for feature design, easily resulting in low computational efficacy and suffering from low predictive performance. To address the limitations, we propose PepBCL, a novel BERT (Bidirectional Encoder Representation from Transformers) -based contrastive learning framework to predict the protein–peptide binding residues based on protein sequences only. PepBCL is an end-to-end predictive model that is independent of feature engineering. Specifically, we introduce a well pre-trained protein language model that can automatically extract and learn high-latent representations of protein sequences relevant for protein structures and functions. Further, we design a novel contrastive learning module to optimize the feature representations of binding residues underlying the imbalanced dataset. We demonstrate that our proposed method significantly outperforms the state-of-the-art methods under benchmarking comparison, and achieves more robust performance. Moreover, we found that we further improve the performance via the integration of traditional features and our learnt features. Interestingly, the interpretable analysis of our model highlights the flexibility and adaptability of deep learning-based protein language model to capture both conserved and non-conserved sequential characteristics of peptide-binding residues. Finally, to facilitate the use of our method, we establish an online predictive platform as the implementation of the proposed PepBCL, which is now available at http://server.wei-group.net/PepBCL/. Availability and implementation https://github.com/Ruheng-W/PepBCL. Supplementary information Supplementary data are available at Bioinformatics online. [ABSTRACT FROM AUTHOR]