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Jalali-Yazdi, F.

Publications and source records attributed to Jalali-Yazdi, F..

2 recordsLinked to original sources

Integrating Diffusion and Liquid AI Models for Predicting Peptide Affinity from mRNA Display Selections

In vitro selection and directed evolution technologies such as mRNA display, explore large libraries ([≥]1014 variants) and generate thousands to millions of functional polypeptide ligands to a variety of targets. Denoising diffusion implicit machine learning models (DDIMs) trained using display-derived deep sequencing data can greatly expand these functional sequences beyond what is accessible experimentally. However, methods are needed to predict peptide properties such as binding free energies ({Delta}G{degrees}). Here, we applied machine learning methods to predict binding free energies of both experimental and DDIM-generated peptide ligands against a target of interest, the oncogenic protein Bcl-xL. To do this, we trained a Closed-form Continuous (CfC) neural network using a dataset of 15,700 peptide ligands where pairs of sequences and their corresponding binding free energies ({Delta}G{degrees}) were used as inputs. This type of model was chosen due to its ability to represent irregular series. The resulting CfC model accurately predicts the rank order, within error, and binding free energies ({Delta}G{degrees}) for both experimental and DDIM-generated peptides, identifying five DDIM-generated peptides with single-digit picomolar affinities. Combining trained DDIM and CfC models offers a unified route to expand the scope of experimental ligand discovery, predict the molecular properties of both experimental and generated ligands, and highlights the utility of large quantitative datasets for making accurate in silico predictions of high-affinity peptide candidates. StatementHigh-throughput sequencing analysis of mRNA display libraries enables generating novel peptide ligands and expands the scope of functional sequences beyond what is accessible experimentally. Closed-form Continuous neural networks trained using sequences and their corresponding free energies accurately predict the binding free energies of both experimental and machine learning-generated peptides, enabling a route to quantitatively predict peptide properties using directed evolution data.

bioengineering↗

Mechanisms for zinc and proton inhibition of the GluN1/GluN2A NMDA receptor

N-Methyl-D-aspartate receptors (NMDARs) play essential roles in memory formation, neuronal plasticity and brain development with their dysfunction linked to a range of disorders from ischemia to schizophrenia. Zinc and pH are physiological allosteric modulators of NMDARs with GluN2A containing receptors inhibited by nanomolar concentrations of divalent zinc and by excursions to low pH. Despite the widespread importance of zinc and proton modulation of NMDARs, the molecular mechanism by which these ions modulate receptor activity has proven elusive. Here, we use cryo-electron microscopy to elucidate the structure of the GluN1/GluN2A NMDAR in a large ensemble of conformations under a range of physiologically relevant zinc and proton concentrations. We show how zinc binding to the amino terminal domain elicits structural changes that are transduced though the ligand-binding domain and result in constriction of the ion channel gate.

biophysics↗