David B. Volkin, PhD

Dr. Volkin is the Ronald T. Borchardt Distinguished Professor of Pharmaceutical Chemistry, and co-founder of the Vaccine Analytics and Formulation Center (VAFC) at The University of Kansas. The VAFC collaborates extensively with partners (non-profits, small/large biopharma/vaccine companies, and academia) on analytical characterization and formulation development projects to facilitate novel candidates entering clinical trials with an emphasis on new candidates for use in the developing world. He has collaborated on the analytical and formulation development of ~100 biotherapeutic and vaccine candidates during ~10 years at KU including now marketed products (recombinant HA flu vaccine (FluBlok™) and an oncolytic herpes virus-based therapy, T-VEC™) as well as late-stage clinical candidates (a live multivalent dengue virus vaccine candidate (TAK-003) and a recombinant non-replicating rotavirus vaccine, NRRV). Dr. Volkin joined the KU faculty in 2010 after a 20-year industry career in vaccine and biopharmaceutical R&D, including senior director level positions at Merck Research Laboratories, Merck & Co. and Centocor R&D, Johnson & Johnson. He led formulation and analytical groups that brought dozens of vaccine and protein drug candidates into human clinical trials, including five vaccines and three monoclonal antibodies approved worldwide for commercial use by regulatory agencies. Dr. Volkin graduated with B.A. in Chemistry from the University of California-San Diego and earned a Ph.D. in Biochemical Engineering from the Massachusetts Institute of Technology. He is co-author of ~175 scientific publications and co-inventor on 15 U.S. patents including patents and papers describing the formulation and stabilization of the commercial HPV (Gardasil™) and rotavirus (RotaTeq™) vaccines. Dr. Volkin was awarded the American Association of Pharmaceutical Scientists (AAPS) Research Achievement Award in Biotechnology in 2015.

A C-terminal Pfs48/45 malaria transmission-blocking vaccine candidate produced in the baculovirus expression system

Characterization of Excipient Effects on Reversible Self-Association, Backbone Flexibility, and Solution Properties of an IgG1 Monoclonal Antibody at High Concentrations: Part 1

Characterization of Excipient Effects on Reversible Self-Association, Backbone Flexibility, and Solution Properties of an IgG1 Monoclonal Antibody at High Concentrations: Part 2

Characterizing and Minimizing Aggregation and Particle Formation of Three Recombinant Fusion-Protein Bulk Antigens for Use in a Candidate Trivalent Rotavirus Vaccine

Effect of Aluminum Adjuvant and Preservatives on Structural Integrity and Physicochemical Stability Profiles of Three Recombinant Subunit Rotavirus Vaccine Antigens

Holistic process development to mitigate proteolysis of a subunit rotavirus vaccine candidate produced in Pichia pastoris by means of an acid pH pulse during fed-batch fermentation

Preformulation Characterization and Stability Assessments of Secretory IgA Monoclonal Antibodies as Potential Candidates for Passive Immunization by Oral Administration

Prophylactic Activity of Orally Administered FliD-Reactive Monoclonal SIgA AgainstCampylobacterInfection

Recombinant Subunit Rotavirus Trivalent Vaccine Candidate: Physicochemical Comparisons and Stability Evaluations of Three Protein Antigens

The Pfs230 N-terminal fragment, Pfs230D1+: expression and characterization of a potential malaria transmission-blocking vaccine candidate