Ahmed Sadek

This study uses systematic K-to-Q mutagenesis to probe the energy landscape of α-Synuclein aggregation, identifying core residue mutations that alter free energy pathways and fibril polymorphism.

This study designs polymorph-specific binders for α-synuclein fibrils using a computational pipeline, demonstrating their utility as selective labeling agents without interfering with fibril dynamics.

The paper identifies 4,500 targetable sites on the human surfaceome and introduces binder seeds for protein design, validated through experimental approaches and supported by a database.

This paper introduces FibrilSite, a computational pipeline to identify structural features of amyloid fibrils, revealing conserved and polymorph-specific sites that guide drug discovery.

The paper introduces a computational framework for fragment-based screening and binding affinity prediction using protein surface descriptors to identify ligands for challenging protein targets.

The paper shows that neighboring post-translational modifications affect the detection of phosphorylated alpha-synuclein at Serine 129 by existing antibodies.