Show simple item record

dc.contributor.advisorFurge, Laura Lowe, 1971-
dc.contributor.authorCho, Christi
dc.descriptionvi, 22 p.en_US
dc.description.abstractCytochrome P450s (P450s) are a superfamily of heme-containing enzymes that are responsible for the metabolism of many xenobiotics and other small endogenous substrates. CYP2D6 is a major P450 enzyme studied during drug development due to its ability to metabolize ~12-20% of all pharmaceuticals. Moreover, there are over 100 allelic variants of CYP2D6 resulting in a wide-range of drug responses among individuals including cases of adverse drug events. The inactivation of one allelic variant, 2D6*53, by a known-mechanism based inactivator, SCH 66712, was investigated in a time- and concentration-dependent manner alongside the reference *1. Though *1 was inactivated by SCH 66712, *53 was not susceptible to inactivation. The greatly decreased rate of inactivation of *53 suggests that inactivation may be dependent on time and positioning of inactivator in the active site. A trapping assay to capture any SCH 66712 reactive intermediates with NAC and GSH was performed, however, the results were inconclusive as analyzed by mass spectrometry.en_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Chemistry Senior Individualized Projects Collection
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder. All rights reserved.
dc.titleInvestigation of the Susceptibility to Inactivation of 2D6*1 and 2D6*53 by a Known Mechanism-Based Inactivator SCH 66712en_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email to request access to this thesis.

Files in this item


This item appears in the following Collection(s)

  • Chemistry Senior Individualized Projects [860]
    This collection includes Senior Individualized Projects (SIP's) completed in the Chemistry Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

Show simple item record