Worcester, MA, Sept. 16, 2012 CellMosaic announced today that it has been awarded a Phase I grant from the National Institute of General Medical Sciences (NIGMS) for the development of new technologies for transient molecular complex characterization. With this award, CellMosaic will develop its proprietary oxLink™ crosslinking reagent kit-method-software package for the identification and quantitation of crosslinked proteins, eventually mapping contact sites at the amino acid level. This Phase I award provides CellMosaic with a total of $159,691 in funds. If early results are promising, the company could receive an additional $1 million in Phase II funding.
“Transient protein–protein interactions play an important role in regulating physiological functions in cells, including gene expression, transport, signal transduction, and cell cycle control. NIGMS understands the importance of transient protein‒protein interactions and the difficulties of studying such interactions.” said Dr. Yumei Huang, founder and CEO of CellMosaic. “We are pleased to receive this NIGMS award. CellMosaic’s oxLink™ will serve as an easy-to-access technology platform for researchers around the globe.”
This award also brings together experts across scientific fields. Dr. Darryl Pappin, associate professor from Cold Spring Harbor Laboratory and an expert in proteomics, will provide high-level consultation services for MS analysis. His lab will also serve as an alpha site for testing the reagents and protocols using his instrumentation. Dr. Judith Klein-Seetharaman, associate professor from University of Pittsburgh and an expert in studying membrane proteins using experimental and computational approaches, will provide valuable advice in the modeling and computation studies, as well as the expression and purification of membrane proteins.
About oxLink™ technologies
oxLink™ technologies combine the experimental approaches of organic chemistry, molecular biology, biochemistry, and biophysics with the computational approaches and system biology. oxLink™ reagents are a set of photocrosslinking reagents with reversible linkage and a segment for MS signature ions. Upon photolysis, carbene generated from oxLink™ forms a covalent bond with the interacting proteins. The crosslinked proteins are digested and the reversible linkage allows efficient purification/enrichment of the crosslinked peptides. Upon fragmentation, these peptides generate signature ions for the identification and quantitation of crosslinked products. A database of oxLink™ modified amino acid residues will be compiled, along with the development of related software tools for MS analysis and molecular modeling. High-throughput sample preparation and analysis will also be explored. If successful, the reagent (oxLink™) and methods will be packaged and commercialized as a kit, serving the global effort in structural studies of transient molecular complexes.
About CellMosaic, LLC
CellMosaic, LLC is an innovator and leader in bioconjugation and crosslinking technologies. Several key technologies are being developed at CellMosaic: oxLink™ technologies for studying protein–protein interactions; superhydrophilic AqueaTether™ linkers for clean conjugation of antibody/protein/peptide/oligo with small molecule drugs; biocompatible, biodegradable, monodispersed AqueaTether™ macromolecules for modification of protein/peptide/oligo drugs and preparation of highly loaded small molecule drugs for better delivery; and bioconjugation platform technologies involving screening, labeling/crosslinking, purification, and analysis of any bioconjugate. The company is also actively engaged in serving biological communities by providing custom synthesis of high quality bioconjugate products. Partnerships and licensing options are available for developing AqueaTether™ based bioconjugate drugs. For more information, please contact Yumei Huang, President & CEO at firstname.lastname@example.org or 508-770-8030.
oxLink™ and AqueaTether™ are trademarks of CellMosaic, LLC
For more information, please visit www.cellmosaic.com