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John P. Marino (Fed)

Group Leader

My research is focused on developing NMR and other biophysical measurements to accurately and precisely define the structure, stability and dynamics of protein and RNA structural folds, ligand complexes and biomolecular interactions at a molecular level.  In addition to enabling fundamental insights into biomolecular structure and function, our work aims to provide a validated measurement infrastructure that supports biopharmaceutical development and regulation.  Our most recent work has focused on the development of NMR techniques for accurate and precise characterization of higher-order-structure (HOS) in biotherapeutics, in particular monoclonal antibodies, which are currently sought by industry for establishing consistency in drug manufacturing, detecting process-related drug-product variations and comparing biosimilars to innovator reference products.  We are developing and demonstrating high-resolution NMR methods as simple, robust spectroscopic approaches for obtaining structural 'fingerprints' of the bioactive form(s) of protein therapeutics at atomic resolution in solution. 

Awards

Department of Commerce Silver Medal Award  2007, 2016 and 2021

Hillebrand Prize 2021

Publications

Interlaboratory Studies using the NISTmAb to Advance Biopharmaceutical Structural Analytics

Author(s)
Katharina Yandrofski, Trina Mouchahoir, M. Lorna De Leoz, David L. Duewer, Jeffrey W. Hudgens, Kyle Anderson, Luke Arbogast, Frank Delaglio, Robert Brinson, John Marino, Karen W. Phinney, Michael J. Tarlov, John E. Schiel
Biopharmaceuticals such as monoclonal antibodies are required to be rigorously characterized using a wide range of analytical methods. Various material

Excipient Innovation Through Precompetitive Research

Author(s)
Bruce Yu, Marc Taraban, Katharine Briggs, Robert Brinson, John Marino
The mRNA COVID-19 vaccines developed by Pfizer/BioNTech and Moderna represent a triumph of vaccine development. The core mRNA component of these vaccines is now

Patents

ClpS BINDING REAGENT FOR PROTEIN SEQUENCING

NIST Inventors
Zvi Kelman and John P. Marino
patent description The invention is a protein-based N-terminal amino acid (NAA) detection reagent. There are three variations of the reagent that bind different N-terminal amino acids with varying affinity and selectivity. The full sequences of the proteins and the binding affinity for each amino

Amino Acid-specific Binder and Selectively Identifying an Amino Acid

NIST Inventors
Zvi Kelman and John P. Marino
patent description The invention is a protein-based N-terminal amino acid (NAA) detection reagent. There are three variations of the reagent that bind different N-terminal amino acids with varying affinity and selectivity. The full sequences of the proteins and the binding affinity for each amino
Created June 18, 2019, Updated December 8, 2022