Regulatory Science
Advice on CMC issues for conducting clinical trials during phases 1, 2, and 3.
Responsible for managing and supervising a Branch in the Office of New Drug Products for the regulatory review processes of INDs and NDAs submitted to three therapeutic areas:
1) Bone, Reproductive and Urologic Products;
2) Dermal and Dental Products;
3) Gastroenterology and Inborn Errors Products;
to ensure that the drug products developed and approved in these areas are manufactured consistently with the federal laws (FD&C Act: Sections; 505, 501, and 502) and regulations (21 CFRs: 314.50, 201, and 210-211) during the drug developments;
and also to assure that, if ready for marketing, the new drugs are available to the patients with the highest possible quality as well as the same safety and efficacy profiles as observed during the pivotal clinical trials.
Managed and supervised the review processes including industry meetings for the CMC sections of INDs and NDAs submitted to the Division of Reproductive and Urologic Drug Products/CDER to assure that the drug products have adequate quality for clinical trials and also, after approval, maintain their quality throughout their life cycles.
As a primary reviewer, CMC sections of INDs, NDAs, and Supplements submitted to the Division of Endocrine and Metabolic Drug Products were reviewed and communicated to the applicants to resolve any disparity from the regulatory requirements found in the submissions.
Mechanism of calcium ion induced prothrombin activation, which is one of the pivotal blood coagulation reactions, was studied using laser induced lanthanide ion fluorescence technique. It has been believed for a long time that calcium ion is bridging prothrombin and platelet to produce thrombin which in turn transform fibronectin to fibrin resulting in clot to stop bleeding. But the laser induced excitation fluorescence data from Tb(III), which replaced Ca(II) in prothrombin, indicate that calcium is not bridging but induce conformational change which then interact with platelet surface.
First application of laser induced lanthanides ion fluorescence spectroscopic technique in elucidating calcium binding sites of calcium binding proteins. The distance between two calcium binding sites was determined by Forster type energy transfer measurements using terbium (III) ion and neodymium (III) ion which were replaced for two calcium ions in calmodulin protein. The results indicated that they were very close to the data from X-ray crystallography. This technique opened a new way of extracting structural information on the metal binding sites in calcium binding proteins without conducting x-ray crystallographic studies.
New drug approval process
13 awards recognized FDA