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Updated: Aug 22, 2026

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
Published on: October 30, 2015
Deep mapping of structural perturbations to energetics enables precise TCR design
Shifu Luo1, Songming Zhang2, Ying Shi3
1Faculty of Health Sciences, University of Macau, Taipa, Macao SAR 999078, China; Faculty of Computer Science and Artificial Intelligence, Shenzhen University of Advanced Technology, Shenzhen, Guangdong, China; Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, Guangdong, China.
None:
Affinity optimization and cross-reactivity profiling are pivotal for T cell receptor (TCR) engineering but remain hindered by repertoire diversity and limited structural insights. We present mpTCRai, a deep learning framework that predicts residue-level structural interactions by simulating the sequential mechanics of antigen presentation and T cell recognition. Through a hotspot-based scoring mechanism, mpTCRai explicitly maps structural perturbations to energetic changes, revealing that these perturbations strongly correlate with experimental affinities (r = -0.88). The model captures the structural dependencies of key molecular switches and computationally screens against cross-reactive mutations like Y5W to evaluate structural off-target risks. Guided by these insights, we computationally prioritized four A6-TCR variants for adult T cell leukemia. Overall, this work establishes a unified computational platform integrating structural and energetic constraints to accelerate the downstream experimental validation and rational design of engineered TCRs.

