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Abstract Insect pests significantly impact global agricultural productivity and crop quality. Effective integrated pest management strategies require the identification of insects, including beneficial and harmful insects. Automated identification of insects under real-world conditions presents several challenges, including the need to handle intraspecies dissimilarity and interspecies similarity, life-cycle stages, camouflage, diverse imaging conditions, and variability in insect orientation. An end-to-end approach for training deep-learning models, InsectNet, is proposed to address these challenges. Our approach has the following key features: (i) uses a large dataset of insect images collected through citizen science along with label-free self-supervised learning to train a global model, (ii) fine-tuning this global model using smaller, expert-verified regional datasets to create a local insect identification model, (iii) which provides high prediction accuracy even for species with small sample sizes, (iv) is designed to enhance model trustworthiness, and (v) democratizes access through streamlined machine learning operations. This global-to-local model strategy offers a more scalable and economically viable solution for implementing advanced insect identification systems across diverse agricultural ecosystems. We report accurate identification (>96% accuracy) of numerous agriculturally and ecologically relevant insect species, including pollinators, parasitoids, predators, and harmful insects. InsectNet provides fine-grained insect species identification, works effectively in challenging backgrounds, and avoids making predictions when uncertain, increasing its utility and trustworthiness. The model and associated workflows are available through a web-based portal accessible through a computer or mobile device. We envision InsectNet to complement existing approaches, and be part of a growing suite of AI technologies for addressing agricultural challenges. 

Abstract Screening amino acid sequence space via experiments to discover peptides that self-assemble into amyloid fibrils is challenging. We have developed a computational peptide assembly design (PepAD) algorithm that enables the discovery of amyloid-forming peptides. Discontinuous molecular dynamics (DMD) simulation with the PRIME20 force field combined with the FoldAmyloid tool is used to examine the fibrilization kinetics of PepAD-generated peptides. PepAD screening of ∼10,000 7-mer peptides resulted in twelve top-scoring peptides with two distinct hydration properties. Our studies revealed that eight of the twelve in silico discovered peptides spontaneously form amyloid fibrils in the DMD simulations and that all eight have at least five residues that the FoldAmyloid tool classifies as being aggregation-prone. Based on these observations, we re-examined the PepAD-generated peptides in the sequence pool returned by PepAD and extracted five sequence patterns as well as associated sequence signatures for the 7-mer amyloid-forming peptides. Experimental results from Fourier transform infrared spectroscopy (FTIR), thioflavin T (ThT) fluorescence, circular dichroism (CD), and transmission electron microscopy (TEM) indicate that all the peptides predicted to assemble in silico assemble into antiparallel β-sheet nanofibers in a concentration-dependent manner. This is the first attempt to use a computational approach to search for amyloid-forming peptides based on customized settings. Our efforts facilitate the identification of β-sheet-based self-assembling peptides, and contribute insights towards answering a fundamental scientific question: “What does it take, sequence-wise, for a peptide to self-assemble?”