Chesapeake PERL To Develop Nanoparticle Linked To Anti-tumor Agent For NCI

C-PERL Will Produce Vault-Chemokine 21 Protein Nanoparticle as a Potential Lung Cancer Therapeutic using Proprietary Protein Production System.

SAVAGE, Md., Oct. 24, 2012 /PRNewswire/ -- Chesapeake PERL has received a Small Business Innovation Research award from the National Cancer Institute to continue development of a protein nanoparticle linked to an antitumor agent as a potential lung cancer therapeutic.  C-PERL collaborators in the laboratory of Dr. Leonard Rome, Professor of Biological Chemistry at UCLA have identified and characterized the vault particle, a unique nanoparticle structure ubiquitous in eukaryotes.  Starting with the Major Vault Protein (MVP), the principal component of vault particles, C-PERL has produced vaults at very high levels in its PERLXpress protein production system.  Under the NCI award C-PERL will formulate MVP with chemokine ligand 21 (CCL21) to form nanocapsules, followed by recovery to very high purity for further characterization and testing.

Preclinical studies conducted by Rome and Dr. Steven Dubinett, Professor & Chief, Division of Pulmonary & Critical Care Medicine, UCLA Department of Medicine  have demonstrated that intratumoral administration of CCL21 gene-modified dendritic cells led to tumor eradication.  C-PERL and its UCLA collaborators believe that recombinant vault nanoparticles linked to CCL21 may be used as a therapeutic for advanced non-small cell lung cancer, circumventing the need to produce autologous dendritic cells.  If successful, this work could substitute a protein therapeutic for a cell-based therapeutic unique for each patient, leading to wider availability and greatly reduced costs.

Chesapeake PERL is a biological manufacturer specializing in the production of high quality proteins, including glycosylated and lipid-associated proteins, multimeric forms and self-assembling macromolecular structures.  PERLXpress, the Company's proprietary, highly automated in vivo implementation of the Baculovirus Expression Vector System, employs whole insect larvae as mini-bioreactors.  The tissue heterogeneity of the insect bioreactors leads to very high levels of protein expression as well as protein modification and processing that closely resemble native versions of the same proteins, and the system flexibility enables rapid, precisely controlled production from micrograms to tens of grams of protein.

Contact:  Dr. George Buchman - 301-317-9300 x104 - [email protected].

SOURCE Chesapeake PERL

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