Akshita Singh

Akshita Singh, Prabesh Paudel, Siddhartha Roy

We introduce a proxy-analyzer framework for detecting hallucinations in large language models. Instead of looking inside the generating model, our system reads already-generated text through a small locally hosted open-weight model and spots hallucinations using the reader's own internal activations. This works just as well when the generator is a closed API like GPT-4 as when it is any open-weight model. We built eighteen features grounded in how transformers process text, covering residual stream norms, per-head source-document attention, entropy, MLP activations, logit-lens trajectories, and three new token-level grounding statistics. We trained a stacking ensemble on 72,135 samples from five hallucination datasets. We tested across seven analyzer architectures from 0.5 billion to 9 billion parameters: Qwen2.5 at 0.5B and 7B, Gemma-2 at 2B and 9B, Pythia at 1.4B, and LLaMA-3 at both 3B and 8B. Across all seven, we consistently beat ReDeEP's token-level AUC of 0.73 on RAGTruth by 7.4 to 10.3 percentage points. Qwen2.5-7B reached an F1 of 0.717, just above ReDeEP's 0.713, while Qwen2.5-0.5B hit 0.706. The most striking finding is how tightly all seven models cluster: AUC spans only 2.3 percentage points across an eighteen-fold difference in model size. Even more surprising, our 3B LLaMA outperforms our 8B LLaMA on RAGTruth, showing that bigger is not always better even within the same model family. Both RAGTruth and LLM-AggreFact include outputs from multiple LLM families, so our results are not skewed toward any particular generator.

Xinyan Zhao, Yi-Ching Tang, Akshita Singh et al.

We introduce AbBiBench (Antibody Binding Benchmarking), a benchmarking framework for antibody binding affinity maturation and design. Unlike previous strategies that evaluate antibodies in isolation, typically by comparing them to natural sequences with metrics such as amino acid recovery rate or structural RMSD, AbBiBench instead treats the antibody-antigen (Ab-Ag) complex as the fundamental unit. It evaluates an antibody design's binding potential by measuring how well a protein model scores the full Ab-Ag complex. We first curate, standardize, and share more than 184,500 experimental measurements of antibody mutants across 14 antibodies and 9 antigens-including influenza, lysozyme, HER2, VEGF, integrin, Ang2, and SARS-CoV-2-covering both heavy-chain and light-chain mutations. Using these datasets, we systematically compare 15 protein models including masked language models, autoregressive language models, inverse folding models, diffusion-based generative models, and geometric graph models by comparing the correlation between model likelihood and experimental affinity values. Additionally, to demonstrate AbBiBench's generative utility, we apply it to antibody F045-092 in order to introduce binding to influenza H1N1. We sample new antibody variants with the top-performing models, rank them by the structural integrity and biophysical properties of the Ab-Ag complex, and assess them with in vitro ELISA binding assays. Our findings show that structure-conditioned inverse folding models outperform others in both affinity correlation and generation tasks. Overall, AbBiBench provides a unified, biologically grounded evaluation framework to facilitate the development of more effective, function-aware antibody design models.