Andrew McShan

Assistant Professor

Georgia Institute of Technology

United States

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Dr. Andrew McShan is an Assistant Professor at the Georgia Institute of Technology in the United States. His research primarily focuses on peptide and protein interactions, biosynthesis in RiPP systems, and the structural modeling of fungal hydrophobins using AlphaFold. He has published extensively on topics including antiviral peptides for SARS-CoV-2 and the biophysical characterization of peptide binding in Plasmodium interactions.

Articles (16)

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2025

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2025

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2025

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2024

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2022

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2021

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2021

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2020

Collaborators (11)

Md Ackas Ali

Graduate Teaching Assistant

Georgia Institute of Technology

UNITED STATES

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Erik Procko

Assistant Professor of Biochemistry

University of Illinois System

UNITED STATES

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Khondaker Miraz Rahman

King’s College London

UNITED KINGDOM

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Mohammed Hossain

University of Melbourne

AUSTRALIA

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Assistant Professor

Georgia Institute of Technology

UNITED STATES

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Andrew McShan

Research Interests

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About

Articles (16)

Extending the Peptide/Protein Interaction Paradigm to a Protein/Protein Engagement Model in RiPP Biosynthesis

Structure-Guided Temporin L Analogs Development to Inhibit the Main Protease of SARS-CoV-2

AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins

Identification and biophysical characterization of Plasmodium peptide binding by common African HLAs

In silico identification and characterization of small molecule binding to the CD1d immunoreceptor

Antiviral peptides inhibiting the main protease of SARS‐CoV‐2 investigated by computational screening and in vitro protease assay

Antiviral fibrils of self-assembled peptides with tunable compositions.

BioDolphin as a comprehensive database of lipid–protein binding interactions

The power and pitfalls of AlphaFold2 for structure prediction beyond rigid globular proteins

Author Correction: Antiviral fibrils of self-assembled peptides with tunable compositions (Nature Communications, (2024), 15, 1, (1142), 10.1038/s41467-024-45193-3)

Discovery and Biosynthesis of Ureidopeptide Natural Products Macrocyclized via Indole N-acylation in Marine Microbulbifer spp. Bacteria.

Utility of methyl side chain probes for solution NMR studies of large proteins

TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules

TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap

Backbone-independent NMR resonance assignments of methyl probes in large proteins

Computational design of closely related proteins that adopt two well-defined but structurally divergent folds

Collaborators (11)

Md Ackas Ali

Erik Procko

Khondaker Miraz Rahman

Mohammed Hossain

Santhamani Ramasamy

Neha Garg

George Burslem

Mohammad Halim

Vinayak Agarwal

Nikolaos Sgourakis

Yunan Luo

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