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Reddy, S. T.

Publications and source records attributed to Reddy, S. T..

At least 19 recordsLinked to original sources

Predicting viral host range for reverse zoonosis surveillance

Zoonotic transmission of viruses has triggered major outbreaks throughout history. However, human-to-animal transmission, or reverse zoonotic transmission, also represents an underappreciated public health threat. Reverse zoonoses can establish novel animal reservoirs that fuel viral evolution and enable eventual spillback into humans, underscoring the importance of defining viral host range. Current approaches for host range prediction are limited. Experimental methods are retrospective and rely on brute-force testing in a small number of models, whereas computational approaches often lack experimental grounding. Here, we present a platform that integrates high-throughput experimental screening with deep learning to predict viral host range from sequence. We screened a yeast-displayed SARS-CoV-2 receptor-binding domain library against 15 ACE2 orthologs from diverse species, and deep sequenced the ACE2-binding and non-binding populations to generate an atlas of 8.8 million unique RBD:ACE2 interaction measurements. These data were used to train a transformer-based deep learning model that predicts RBD:ACE2 compatibility across animal species from sequence alone, and generalizes in a zero-shot manner to ACE2 orthologs not observed during training. Critically, the model pairs each prediction with a distance-based uncertainty estimate, allowing hundreds of candidate species to be triaged by both predicted host compatibility and confidence. This framework enables the rapid prioritization of animal species for SARS-CoV-2 surveillance and provides a general strategy for anticipating viral host range.

bioengineering↗

Generative Drug Design in a Loop with dtSFM

Directed evolution consisting of iterative rounds of diversification, selection, and counter-selection, underlies modern protein and antibody engineering, yet small-molecule drug design still advances largely through high-throughput screening and medicinal-chemistry intuition. Transformer softmax attention is mathematically identical to the Boltzmann distribution that governs molecular binding at thermal equilibrium1, an isomorphism that prescribes a sequence-native Specificity Foundation Model (SFM)2. This framework was recently applied across seven molecular recognition domains3,4 and scaled into the drug-target SFM (dtSFM), the first to pair a full-scale encoder with a generative decoder5. Whether such a model can be driven, iteratively and under selection, to optimize leads rather than sample them once has not been shown. Here we present GenLoop, a closed generative drug design loop that turns single-pass generation into directed evolution of chemistry. dtSFM generates target-conditioned molecules and reranks them by their thermodynamic compatibility score. An orthogonal structural verifier, AlphaFold 3, is used that shares no architecture or training data with dtSFM. Cheminformatics filters enforce developability, and generative evolution is performed on the structurally verified candidates, selecting for predicted binders and counter-selecting against off-target chemistry. Applied across twelve drug targets spanning pharmacologically distinct mechanism classes, GenLoop produced AlphaFold 3-verified designs that reached the structural confidence of the approved drug for five of the twelve targets, with the best designs at interface iPTM 0.93-0.98 and PAE 0.8-2.0 [A], as well as resolving paralog selectivity across nine targets. Two full disease campaigns followed. For the cystic-fibrosis transmembrane conductance regulator, GenLoop designed nine developability-filtered and structurally novel lead candidates (iPTM up to 0.93, interface PAE 2.3 [A]) targeting all three orthogonal sites of the approved drug Trikafta. For the GLP-1 receptor family, dtSFM engineered tunable single-, dual-, and triple-receptor incretin designs, yielding 23 central-pocket candidates that are structurally novel at median iPTM 0.89 and interface PAE 1.95 [A]. GenLoop with dtSFM brings directed evolution to small molecules through computational-thermodynamic selection; wet-lab validation is the immediate next step.

synthetic biology↗

Breaking the Synthesis Barrier for AI-Designed DNA Libraries

Designing DNA libraries is a key challenge from drug design to protein engineering and synthetic biology. Modern generative models offer opportunities to navigate the design space and propose specific sequences predicted to be effective in-silico. Designing deterministic libraries of specific sequences is however limited by the cost of DNA synthesis - the synthesis barrier. In contrast, high-throughput multiplexed screening can measure the function of billions of biological sequences in parallel. Harnessing this technology requires the design of randomized libraries with specific design constraints to achieve low synthesis costs. In practice, such stochastic libraries are often chosen heuristically, sacrificing control for scale. Is there a way to bridge AI-based in-silico sequence design with high-throughput experimentation? In this work, we introduce Policy Gradients for Library Design (PGLD). PGLD uses a synthesis-aware parametrization of stochastic DNA libraries and optimizes them against a specified objective function. This allows for designing massive, controlled libraries without being limited by synthesis costs. We show how PGLD enables lab-in-the-loop design of multi-round high-throughput experiments, and large-scale in-vitro DNA sampling from generative models. Finally, we use PGLD to design a library of ~ 106 unique sequences which is synthesized at a cost of ~ 700 USD to explore the mutation space of a broadly neutralizing influenza antibody.

bioengineering↗

A Drug-Target Specificity Foundation Model for Off-target Prediction, Repurposing, and Generative Design

Molecular recognition - which small molecule binds which protein, and with what selectivity - governs the efficacy, safety, and discovery of every therapeutic, yet binding specificity is still determined by experimental screening or by computational methods that first predict three-dimensional structure. Transformer softmax attention is mathematically isomorphic to the Boltzmann distribution governing molecular binding at thermal equilibrium1, an identity that prescribes a single sequence-native architecture: the Specificity Foundation Model (SFM), which computes molecular binding compatibility as a thermodynamic quantity directly from sequence2. The framework was recently realized as prototype encoders across six molecular-recognition domains3. Here we report the small molecule drug-target protein SFM (dtSFM) as the first instance to pair a full-scale encoder with a generative decoder, trained on publicly available data consisting of 714,747 measured drug-protein interactions spanning 522,776 compounds and 22,964 proteins. Throughout, we verify binding predictions with AlphaFold 34 as an orthogonal structural verifier that shares no architecture, training data, or representational basis with dtSFM. From this single dtSFM model we demonstrate the three sequence-native applications of drug discovery: off-target prediction, repurposing, and generative design. The dtSFM encoder retrieves a drugs target, and a targets drug, at 95% and 89% recall-at-10 in distribution, respectively. In the drug[->]target direction it screens off-targets at proteome scale, ranking the documented off-targets of clinical kinase inhibitors at a median of 30th out of 4,910 genes - the top 0.6% of the screen - when validated against a chemoproteomic panel5. In the target[->]drug direction it ranks the full 522,776-compound library against three immunology targets, identifying 46 novel candidates that pass AlphaFold-3 structural gating. The dtSFM cross-attentive decoder generates novel molecules for 16 targets, 850 of 1,200 (71%) designed candidates match the AlphaFold 3 structural confidence of the approved drug (iPTM [≥] 0.9 and interface PAE [≤] 1.67 [A]), with the best candidates reaching iPTM 0.95-0.99 and interface PAE 0.79-1.37 [A]. dtSFM brings computational thermodynamics to every stage where molecular recognition shapes drug discovery; experimental wet-lab validation is the immediate next step.

synthetic biology↗

Vibe Coding Specificity Foundation Models

Molecular recognition -- the determination of which agent binds which target -- governs adaptive immunity, gene regulation, signal transduction, RNA silencing, enzyme catalysis, and the selectivity of therapeutics. Determining binding specificity remains dependent on experimental screening or domain-specific computational tools that do not generalize across binding modalities. Transformer softmax attention is mathematically identical to the Boltzmann distribution governing molecular binding1. This identity, together with five conditions of molecular recognition systems, prescribes a single neural network architecture for cross-modal binding prediction: dual sequence encoders, symmetric contrastive learning, and a learned physical temperature2. A Specificity Foundation Model (SFM) is an instance of this physics-derived, sequence-to-sequence architecture that maps any agent-target sequence pair to a binding compatibility score, enabling bidirectional retrieval across molecular recognition domains without requiring structural information. The first SFM for antibody-antigen binding demonstrated [~]100,000-fold greater data efficiency than comparable vision-language models3. Here we report six SFMs across six molecular recognition domains -- transcription factor-DNA, enzyme-substrate, peptide-MHC, CRISPR gRNA-off-target genomic DNA, microRNA-mRNA target, and small molecule drug-target protein -- using the identical architecture without modification and trained using publicly available data only. Evaluated by cross-modal retrieval from pools of 512 candidates (random baseline 0.2%), in-distribution R@1 ranges from 27.7% to 98.0% across the six domains. mir-SFM retrieves miRNA targets at 98.0% R@1, including the [~]80% of validated interactions that seed-matching tools cannot find. mhcSFM achieves 95.4% R@1 on held-out rare HLA alleles absent from training. Applying crisprSFM to CRISPR off-target prediction improves precision to 94.0% compared to 33.2% from Hamming distance alone. All six SFMs were built by a domain expert with no programming experience using vibe coding -- natural-language-directed AI coding agents -- with numerical claims independently verified by an orthogonal AI auditor. These results establish SFMs as a physics-derived, sequence-native class of model that augments experimental and computational workflows across molecular recognition domains.

synthetic biology↗

Methods for Molecular Recognition Computing

The softmax attention mechanism in transformer architectures (Vaswani et al., 2017) is mathematically identical to the Boltzmann distribution governing molecular binding at thermal equilibrium (Boltzmann, 1877). Luces Choice Axiom (1959) establishes this function - which we term the convergence equation - as the unique function satisfying five axioms of competitive selection: positivity, normalization, unrestricted domain, rank preservation, and independence of irrelevant alternatives. We show that five additional architecture conditions - discrete intermolecular contacts, bilinear energy decomposition, finite competitor pools, thermal equilibrium, and stochastic selection - are satisfied by at least ten biological molecular recognition systems and together prescribe a complete neural architecture: dual encoders, cross-attention, InfoNCE contrastive training, symmetric loss, learned temperature, and cross-attentive decoder. We term this architecture a Specificity Foundation Model (SFM) and specify it for antibody-antigen, TCR-peptide-MHC, transcription factor-DNA, microRNA-mRNA, enzyme-substrate, CRISPR guide RNA-DNA, drug-target, peptide-MHC, receptor-ligand, and RNA-binding protein-RNA recognition. The first implementation (CALM; Lee et al., 2026) achieves antibody-antigen retrieval from approximately 4,000 training pairs with [~]100,000-fold greater data efficiency than comparable contrastive architectures trained without the physics derivation. We classify this as Level 3 architecture-physics alignment and derive three further theoretical results: an exponential scaling law for retrieval accuracy as a function of training data diversity (the MRC scaling law), a two-parameter affinity calibration framework connecting contrastive scores to binding free energies, and a hybrid recursive learning framework for cross-modal reinforcement learning with orthogonal verification. The failure conditions of the framework are analyzed in terms of the validity of equilibrium thermodynamics for molecular binding and the convergence properties of gradient-based parameter estimation.

synthetic biology↗

Contrastive learning for antibody-antigen sequence-to-specificity prediction

Predicting which antibodies bind to which antigens directly from primary amino acid sequences remains a major challenge, as no current method can reliably determine this specificity at both a repertoire and proteome scale. Structure-based protein design frameworks can propose antibody binders to specified antigenic epitopes, but they do not solve the "sequence-to-specificity" task of mapping antibodies to cognate epitopes, and vice versa. Here, we introduce CALM (Cross-attention Adaptive Immune Receptor-Antigen Language Model), a dual-encoder plus cross-attentive decoder architecture that treats antibody-antigen recognition as molecular translation. Using contrastive learning, antigen and antibody encoders learn a shared embedding space that aligns cognate epitope-paratope binding pairs. CALM-1.0 is trained and evaluated on 4,138 curated antibody-antigen pairs obtained from the PDB-derived structural antibody database (SAbDab). On a leakage-controlled test split drawn from sequence clusters at 80% identity and unseen during training, CALM-1.0 achieves a mean top-1 retrieval (R@1) of 7%, with consistent performance across both directions (Ab[->]Ag and Ag[->]Ab). CALM establishes a foundation for bidirectional antibody-antigen sequence-to-specificity prediction with the potential to unify retrieval and generative design.

immunology↗

Computational Convergence of Adaptive Immunity and Artificial Intelligence

The adaptive immune system and modern artificial intelligence (AI) have independently converged on identical computational strategies for solving the recognition and generalization problem: learning to identify which inputs should be associated with which outputs, such that performance extends to novel instances never seen during training. We demonstrate that four major AI architectural innovations can be derived from immunological first principles. Two represent exact mathematical equivalences: the softmax function in transformer attention is the Boltzmann distribution governing antibody-antigen binding; the InfoNCE loss in contrastive learning is the negative log of clonal selection probability. Two represent strategic convergences: the pre-training/fine-tuning/RLHF training hierarchy parallels the germline/somatic hypermutation/T follicular helper stages of antibody affinity maturation; retrieval-augmented generation mirrors the long-lived plasma cell and memory B cell dual memory system. Critically, these derivations run from immunology to AI, not the reverse--the mathematical structures of transformer attention and contrastive learning could have been derived from immunological first principles before their empirical discovery in AI. The framework generates testable predictions for immune specificity foundation models and suggests that certain computational strategies may be fundamental to any system solving recognition and generalization under resource constraints. Modern AI has independently converged on computational strategies that the adaptive immune system discovered through 500 million years of evolution. One-sentence summaryThe mathematics of transformer attention and contrastive learning can be derived from the biophysics of immune recognition.

immunology↗

Generative design of antibody Fc-variants with synthetic and programmable functional profiles

Beyond antigen recognition, antibodies direct diverse immune effector functions through their constant (Fc) domain. While the Fc domain is central to antibody biology and therapeutic efficacy, our understanding of how Fc sequence encodes function remains limited, as most of Fc sequence space has not been experimentally mapped or linked to Fc-receptor engagement. Furthermore, the extensive overlap in Fc-receptor binding sites on the Fc domain has impeded efforts to engineer antibodies with tailored, multi-receptor engagement profiles that can precisely control downstream immunity. Here we introduce a novel framework for Fc engineering that integrates protein engineering with deep learning to rationally predict and engineer antibody Fc function. Using a yeast-based, aglycosylated Fc display system, we performed deep mutational scanning across the entire human IgG1 Fc domain, allowing the rational design of a diverse combinatorial library of more than 108 Fc-variants. This library was sorted based on binding to a panel of eight canonical Fc-receptors, and the resulting populations were deep sequenced to generate a high-quality dataset comprising millions of unique Fc sequences annotated with their respective Fc-receptor binding profiles. Deep learning-based classifiers trained on this dataset accurately predicted Fc-receptor binding activity from Fc sequence across all Fc-receptors tested. We further developed FcGPT, a domain-specific autoregressive protein language model pre-trained on over three million unique Fc sequences, and refined by post-training through reinforcement learning with experimental feedback (RLXF) and synthetic verifiers. FcGPT enables the computational design of novel Fc-variants with user-defined Fc-receptor binding profiles, providing a foundational tool for understanding and programming antibody-mediated immunity.

bioengineering↗

A yeast mating-based platform enables the generation and screening of ultra large antibody libraries

Yeast display is a powerful platform for antibody engineering, offering eukaryotic protein folding and compatibility with fluorescence-activated sorting (FACS). However, conventional yeast display faces limitations in terms of library size and display heterogeneity due to plasmid-based expression. Here, we present a yeast display platform that combines genomic library integration and high-efficiency mating to generate ultra-diverse antibody libraries approaching the diversity of phage-libraries (>1011). We engineered two yeast strains, LFYa and LFYalpha, featuring genomically integrated landing pads for high-efficiency library insertion. To enable compatibility with deep sequencing, we integrated the recombinase BxB1, which links heavy (HC) and light chain (LC) information onto a single chromosome. Using our platform, we constructed synthetic antibody libraries with HC and LC diversities of 4.1x107 and 1.7x107 variants, respectively and with an improved mating protocol, we achieved a combinatorial library diversity exceeding 1011. We demonstrated that genomic integration yields uniform surface display. Screening this antibody library against multiple antigens resulted in the discovery of binders with affinities in the single-digit nanomolar to picomolar range, demonstrating the platforms utility for the discovery of antibodies with therapeutically relevant affinities. This work establishes a robust and deep sequencing-compatible yeast display system that overcomes key limitations of previous mating-based platforms.

bioengineering↗

High-throughput cell-free profiling of SARS-CoV-2 RBD variants enables rapid and quantitative in vitro affinity landscape mapping

SARS-CoV-2 variants continue to threaten public health, necessitating the study of cumulative and epistatic effects of receptor-binding domain (RBD) mutations on antibody evasion. We present a high-throughput platform combining cell-free protein synthesis and microfluidics to quantify the affinity of a large number of RBD triplet mutants covering the evolutionary space between wild-type and Omicron against two therapeutic antibodies and one engineered binder. Using rapid in vitro gene assembly and cell-free synthesis, we expressed 518 RBD variants and obtained 31,740 quantitative affinity measurements to generate three comprehensive binding energy landscapes. This approach enables rapid and large-scale in vitro affinity profiling and machine learning-based predictions, providing a valuable tool for studying emerging variants.

systems biology↗

Predicting TCR antigen specificity at proteome-scale with synthetic immune cells and machine learning

TCR specificity to peptide-HLA antigens is central to immunology, impacting responses in infection, autoimmunity and cancer. Achieving precise recognition while avoiding off-target reactivity is critical for effective immunity and safe therapeutic interventions. Comprehensive, proteome-wide specificity profiling of TCRs is challenging with current methods, which notably lack integrated machine learning for large-scale analysis. Here, we report a synthetic immune cell system coupled with machine learning to enable TCR functional and specificity mapping of peptide-HLA antigens at proteome-scale. Multi-step immunogenomic engineering of synthetic antigen-presenting cells (APCs) was performed to enable stable mono-allelic integration and precise display of peptide antigens and HLA class I from a defined genomic locus, ensuring genomically-encoded antigen presentation. Compatible with a synthetic TCR displaying T cell system, this platform incorporates a fluorescent reporter of cytokine-mediated signaling for real-time activation detection in both synthetic APCs and T cells. We combined this screening with diverse peptide antigen libraries and deep sequencing to train supervised machine learning models. These models were applied to predict TCR specificity to peptide-HLA antigens across the entire human proteome. Experimental validation confirmed novel off-targets for therapeutic TCR candidates, including for a clinically-approved TCR therapeutic. This integrated synthetic immune cell and machine learning approach provides unprecedented proteome-wide peptide-HLA specificity mapping to support the development of safer TCR-based therapies. One sentence summaryWe present a synthetic immune cell platform integrated with machine learning that enables prediction of TCR specificity to peptide-HLA antigens at proteome-scale.

immunology↗

Screening of a pooled library of chimeric antigen receptor T cells based on secretory function

Chimeric antigen receptor (CAR) T cell therapies have shown promise in treating hematologic malignancies, but challenges remain due to immune suppression, antigen heterogeneity, and insufficient functional screening platforms. Here, we present a modular nanovial-based platform for high-throughput, single-cell functional screening of pooled CAR T cell libraries. Nanovials, hydrogel microparticles with nanoliter-scale cavities, were functionalized with recombinant HER2 antigen and cytokine-capture antibodies to simulate antigen-presenting cells and capture secreted interferon-{gamma} (IFN{gamma}). This system enabled the selective capture, activation, and functional profiling of CAR T cells based on antigen engagement and cytokine secretion. We screened a 32-variant CAR library with diverse intracellular signaling domains, using nanovials to isolate IFN{gamma}-secreting cells after 3- and 12-hour CAR-specific stimulation. IL15RA-containing CARs, particularly IL15RA-CD28, were preferentially enriched in the sorted T cells after 3 hours of stimulation, consistent with early effector activation profiles. By 12 hours, IL15RA-containing constructs remained enriched while other CD40-containing domains showed delayed but substantial enrichment, suggesting prolonged signaling dynamics. The platforms high-throughput capability (>2 million cells screened), compatibility with downstream sequencing, and tunable antigen presentation make it ideal for identifying CAR constructs associated with various time-dependent secretion phenotypes.

bioengineering↗

Dissecting serum polyclonal antibody escape to SARS-CoV-2 variants by deep mutational learning

The rapid emergence of SARS-CoV-2 variants harboring multiple receptor-binding domain (RBD) mutations continues to challenge the efficacy of vaccines and antibody therapeutics. While deep mutational scanning (DMS) has been instrumental in mapping single-mutation effects on antibody binding and immune escape, it remains limited in its ability to assess combinatorial mutational landscapes. Here, we extend deep mutational learning (DML), a method integrating combinatorial mutagenesis, yeast surface display, deep sequencing, and machine learning, to analyze serum polyclonal antibody escape. Human sera from COVID-19-vaccinated individuals were screened against diverse RBD variant libraries, validating 300 serum-variant interactions across 10 individuals by comparing predicted and observed binding to 30 RBD variants, confirming accurate mapping of binding and escape profiles. Model performance remained consistent across machine learning architectures, suggesting that serum binding and escape are governed by distinct, localized RBD sequence features. Notably, escape profiles were highly individualized, whereas binding signatures were more conserved, reflecting convergent epitope targeting. This approach highlights the potential of DML to generalize beyond observed RBD variants, assess cohort-specific immune breadth, and inform vaccine and therapeutic design in the face of viral evolution.

immunology↗

Delineating inter- and intra-antibody repertoire evolution with AntibodyForests

MotivationThe rapid advancements in immune repertoire sequencing, powered by single-cell technologies and artificial intelligence, have created unprecedented opportunities to study B cell evolution at a novel scale and resolution. However, fully leveraging these data requires specialized software capable of performing inter- and intra-repertoire analyses to unravel the complex dynamics of B cell repertoire evolution during immune responses. ResultsHere, we present AntibodyForests, software to infer B cell lineages, quantify inter- and intra-antibody repertoire evolution, and analyze somatic hypermutation using protein language models and protein structure. Availability and implementationThis R package is available on CRAN (1) and Github at https://github.com/alexyermanos/AntibodyForests, a vignette is available at https://cran.case.edu/web/packages/AntibodyForests/vignettes/AntibodyForests_vignette.html

bioinformatics↗

High-Throughput Antibody Neutralization Screening in Massively Parallel Droplet Arrays

Neutralizing antibodies provide rapid immune defense against infectious diseases, but are difficult to discover at scale because neutralization assays require live reporter cells and soluble monoclonal antibodies. Here we report Droplet Reporter Cell Testing for Neutralization (DrReCT-Neutralization) to screen antibody gene libraries for their ability to neutralize viral infections. We established the necessary engineered cell lines and validated the DrReCT screening platform using synthetic oligoclonal libraries, followed by an example discovery campaign that demonstrated scalable functional antibody data collection against viral diseases.

immunology↗

PLMFit : Benchmarking Transfer Learning with Protein Language Models for Protein Engineering

Protein language models (PLMs) have emerged as a useful resource for protein engineering applications. Transfer learning (TL) leverages pre-trained parameters to extract features to train machine learning models or adjust the weights of PLMs for novel tasks via fine-tuning through back-propagation. TL methods have shown potential for enhancing protein predictions performance when paired with PLMs, however there is a notable lack of comparative analyses that benchmark TL methods applied to state-of-the-art PLMs, identify optimal strategies for transferring knowledge and determine the most suitable approach for specific tasks. Here, we report PLMFit, a benchmarking study that combines, three state-of-the-art PLMs (ESM2, ProGen2, ProteinBert), with three TL methods (feature extraction, low-rank adaptation, bottleneck adapters) for five protein engineering datasets. We conducted over >3,150 in silico experiments, altering PLM sizes and layers, TL hyperparameters and different training procedures. Our experiments reveal three key findings: (i) utilizing a partial fraction of PLM for TL does not detrimentally impact performance, (ii) the choice between feature extraction and fine-tuning is primarily dictated by the amount and diversity of data and (iii) fine-tuning is most effective when generalization is necessary and only limited data is available. We provide PLMFit as an open-source software package, serving as a valuable resource for the scientific community to facilitate the feature extraction and fine-tuning of PLMs for various applications. ONE SENTENCE SUMMARYPLMFit is a comparative analysis aimed at identifying the most effective strategies for transfer knowledge from protein language models by benchmarking fine-tuning techniques on a range of protein engineering tasks.

bioinformatics↗

Antibody affinity engineering using antibody repertoire data and machine learning

Advanced antibody discovery and engineering workflows take advantage of the combination of high-throughput screening, deep sequencing and machine learning (ML). Most high-throughput methods, however, lack the resolution to provide absolute affinity values of antibody-antigen interactions, limiting their utility for precise engineering of binding kinetics. In this study, we utilize antibody repertoire data, affinity characterization and ML for antibody affinity engineering. Leveraging natural antibody sequence information from repertoires of immunized mice, we identified and experimentally measured affinities for 35 antigen-specific variants. Supervised ML models trained on these sequences achieved remarkable accuracy in predicting affinity, despite the limited dataset size. We utilized the trained ML model to in silico-design eight synthetic antibody variants, of which seven exhibited the desired affinities. Our study illustrates the potential of this streamlined and efficient approach for precise engineering of the affinity of antibodies while reducing extensive experimental screening.

bioengineering↗