Its a most regal honour for an academic.

On November 17, Oceanography Professor John Cullen and Biochemistry and Molecular Biology Professor Andrew Roger will become fellows of the Royal Society of Canada (RSC). Induction into the RSC represents a distinguished career in research the cumulative accomplishments of an academic life. Fellows are considered top intellectuals, persons who provide thought leadership for the betterment of Canada and the world.

This honour comes for Dr. Cullen after years of presenting solid research on significant global challenges. Just one example is his work on human-caused stratospheric ozone depletion, a hot-button issue in the 1980s and 90s. Although at the time scientists knew increased ultraviolet radiation from ozone depletion would harm marine organisms, they didnt know by how much.

I worked with Dr. Patrick Neale at the Smithsonian Institute and Richard Davis in my lab to develop new ways to measure the effects of ultraviolet radiation on photosynthetic plankton, explains Dr. Cullen. We discovered that UV radiation would cause significant but not catastrophic impacts and in doing so we developed a sound scientific foundation for making those assessments.

Dr. Roger has spent much of his career piecing together the Tree of Life. His group has shown that much of lifes diversity comprises five-to-six super-kingdom level groups that diversified more than 1 billion years ago. In collaboration with Alastair Simpson's Biology group, Rogers team assembled the first evidence for a large super-kingdom group called the Excavata.

Clarifying the deepest 'structure' of the Tree of Life is realizing many biologists dreams since Darwin proposed the theory of evolution, says Dr. Roger. We can now map major evolutionary transitions that gave rise to diversity and better understand mechanisms that control evolution.

Drs. Cullen and Roger agree that their success stems from an unwavering dedication to uncovering the truth.

Dr. Cullen emphasizes reporting results honestly and clearly, reiterating, A scientists job is to help people understand nature, not to impress people with accomplishments.

Dr. Roger draws on collaborations with other academics, postdoctoral researchers and students to find the truth behind lifes mysteries. He credits much of his success to seeking out academics with complementary skills and getting the right trainees for his projects.

Ive been fortunate to work with excellent colleagues and trainees, says Dr. Roger. Ive also strived to create a comfortable intellectual environment and provide the financial support and guidance for my trainees to explore their scientific interests.

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A "Royal" recognition for Dal scientists

Two UC Santa Barbara professors have been named recipients of the American Chemical Societys 2013 national awards for professionaladvancement. Peter C. Ford, professor in the Department of Chemistry and Biochemistry, and Craig J. Hawker, also a professor in the Department of chemistry and Biochemistry,professor of materials, and director of the Materials Research Laboratory, have been named among the 64 award winners from across the country

In only one other year, 1996, did UCSB have more than one winner of theAmerican Chemical Society (ACS) awards. The awards will be presented at the nationalACS meeting in New Orleans in April.Ford is the recipient of the ACS Award for Distinguished Service in the Advancement of Inorganic Chemistry. This award recognizes individuals who haveadvanced inorganic chemistry by significant service, in addition to performingoutstanding research. It is sponsored by StremChemicals.

I am of course very pleased and honored to have received this award from my colleagues in the American Chemical Society, saidFord.

Since this is largely in recognition of the body of work generated by my graduate and postdoctoral students and collaborators over my tenure at UCSB, I consider it an award to my research group collectively as well as another testament to the high regard in which this campus is nowheld. I am proud to be aGaucho.

Hawker has been named recipient of the ACS Award in Polymer Chemistry. Thecitation states that Hawker was nominated for transforming the field of polymer chemistry through the clever adaptation of synthetic organic chemistry concepts and theadvancement of macromolecular engineering. ExxonMobil Chemical Company sponsored thisaward.

I am thrilled with the award and the recognition that it brings to my students, collaborators, and co-workers, as well as to the unique research environment at UCSB, said Hawker. The sustained success of cross-disciplinary research has been a key driver in reinforcing UCSBs international standing in the materials chemistry arena. I am grateful for the enormous benefits that this proud tradition has bought to myresearch.

Ford joined the faculty at UCSB in 1967 after earning his Ph.D. at Yale and completing a National Science Foundation postdoctoral fellowship with Nobel laureateHenry Taube at Stanford University. He is a Fellow of the American Association for theAdvancement of Science and was a Senior Fulbright Fellow. His awards include a Dreyfus Foundation Teacher-Scholar Award in 1972; the Alexander von Humboldt Foundation Senior U.S. Scientist Award in 1992; the Richard C. Tolman Medal of theACS in 1993; and the Inter-American Photochemical Society Award in Photochemistry in2008.

Hawker received his Ph.D. from the University of Cambridge, and then completeda postdoctoral fellowship with Jean M. J. Frchet at Cornell. In 2004, he moved from theIBM Almaden Research Center to join the faculty at UCSB. Some of his recent awardsinclude the 2012 Centenary prize from the Royal Society of Chemistry; the 2011 Arthur C. Cope Scholar from the American Chemical Society; and the 2008 DSM PerformanceMaterials Award from the International Union of Pure and Applied Chemistry. In 2010,he was named a Fellow of the RoyalSociety.

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UCSB Professors Receive National Chemistry Awards

FORT COLLINS, Colo.--(BUSINESS WIRE)--

Optiferrin, a recombinant human transferrin (rhTF) protein produced by Ventria Bioscience using ExpressTec, has been shown to be biochemically and structurally similar to human transferrin (hTF) molecules derived either from human serum or a recombinant mammalian expression system, according to a paper published today in the Journal of Inorganic Biochemistry.1 Optiferrin is sold commercially by InVitria, the bioreagents division of Ventria Bioscience, for use in cell culture applications.

Recombinant human transferrin used in cell culture media supplements is available from a number of commercial sources, but characterization of these products rarely goes beyond a crude assessment of purity by gel electrophoresis, said Dr. Anne B. Mason, Research Professor of Biochemistry at the University of Vermont (Burlington, Vt.) and the senior author on the study. Functional validation by more thorough and quantitative methods such as ours is essential for either analytical purposes or for pharmaceutical development.

The paper, titled Biochemical and Structural Characterization of Recombinant Human Serum Transferrin from Rice (Oryza sativa L.), was the result of a collaboration between researchers at the University of Vermont College of Medicines Department of Biochemistry; the University of Massachusetts at Amhersts Department of Chemistry, (Amherst, Mass.); Ventria Bioscience; and InVitria. The research team used a battery of biochemical and biophysical techniques to compare the functional properties of Optiferrin to either native hTF purified from human serum, or a reference form of recombinant N-His-tagged nonglycosylated human transferrin (referred to as N-His hTF). As authorities on the biochemical properties of proteins involved in iron metabolism, Dr. Masons group had previously developed and characterized the mammalian expression system used to produce the N-His hTF protein and mutant variations and also developed many of the biophysical techniques used in this study as part of their ongoing research.

The in-depth biochemical and structural characterization analysis included techniques such as peptide mapping and capillary liquid chromatography with tandem mass spectrometry; circular dichroism spectrometry; ultraviolet-visible (UV-vis) spectroscopy; determination of molar absorption coefficient for iron; steady-state tryptophan fluorescence; relative transferrin-receptor binding affinity; and iron release under simulated endosomal conditions. The results demonstrated that Optiferrin is biochemically and structurally similar to hTF, exhibiting the tight but reversible binding to iron (Fe3+) that is a hallmark of transferrin function.

Human transferrin, either purified from human blood serum or biomanufactured using various recombinant protein expression systems, is widely used in biomedical research and the biotechnology industry as a supplement to support mammalian cell growth in serum-free cell culture media. It also has potential therapeutic uses in the treatment of thalassemia, atransferrinemia, and age-related macular degeneration, and as an anti-cancer drug delivery molecule. However, hTF sourced from serum poses the risk of transmission of blood-borne pathogens, while current systems for recombinant expression are difficult to scale in a cost-effective manner for biopharmaceutical applications. Thus a cost-efficient production method is desirable. The authors of the present study performed a basic economic analysis of current rhTF biomanufacturing methods (Table S1) and found that rhTF produced using Ventria Biosciences ExpressTec technology is dramatically more cost effective than other commercial methods, including yeast, immortalized human cell lines (HEK293), or wheat germ.

While we have long known that Optiferrin supports optimal cell growth in serum-free media, this study provides further validation that recombinant human transferrin produced using our ExpressTec technology functions similarly to its endogenous counterpart, said Scott Deeter, president and CEO of Ventria Bioscience. These results will support our future efforts toward developing a cost-effective, biopharmaceutical-grade human transferrin product.

1 Full citation: Steere AN, Bobst CE, Zhang D, Pettit S, Kaltashov IA, Huang N, Mason AB. Biochemical and structural characterization of recombinant human serum transferrin from rice (Oryza sativa L.). J Inorg Biochem. 2012;116:37-44. doi: 10.1016/j.jinorgbio.2012.07.005.

About InVitria

InVitria develops, manufactures and markets a portfolio of animal-free cell culture supplements that improve performance, cost effectiveness and consistency of cell-based biomanufacturing systems. InVitria is a division of Ventria Bioscience. For more information, visit http://www.invitria.com.

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Study Shows Optiferrin™ Recombinant Human Transferrin Is Comparable to Serum-Derived or Mammalian-Expressed Transferrin

Public release date: 24-Sep-2012 [ | E-mail | Share ]

Contact: John Tomich jtomich@k-state.edu 785-532-5956 Kansas State University

MANHATTAN, Kan. -- Kansas State University researchers have discovered a molecule that may be capable of delivering drugs inside the body to treat diseases.

For the first time, researchers have designed and created a membrane-bounded vesicle formed entirely of peptides -- molecules made up of amino acids, the building blocks of protein. The membrane could serve as a new drug delivery system to safely treat cancer and neurodegenerative diseases.

A study led by John Tomich, professor of biochemistry at Kansas State University, has been published in the journal PLOS ONE in September, and a patent for the discovery is pending.

The peptides are a set of self-assembling branched molecules made up of naturally occurring amino acids. The chemical properties of a peptide create a vesicle that Tomich describes as a bubble: It's made up of a thin membrane and is hollow inside. Created in a water solution, the bubble is filled with water rather than air.

The peptides -- or bubbles -- can be made in a solution containing a drug or other molecule that becomes encapsulated as the peptide assembles, yielding a trapped compound, much like a gelatin capsule holds over-the-counter oral remedies. The peptide vesicles could be delivered to appropriate cells in the body to treat diseases and minimize potential side effects.

"We see this as a new way to deliver any kind of molecule to cells," Tomich said. "We know that in certain diseases subpopulations of cells have gone awry, and we'd like to be able to specifically target them instead of attacking every cell, including healthy ones."

The finding could improve gene therapy, which has the potential to cure diseases by replacing diseased cells with healthy ones. Gene therapy is being tested in clinical trials, but the biggest challenge is how best to deliver the genes.

Methods include cells with a virus being injected into the body, and liposomes -- fatty compounds -- carrying the genes. However, these methods may present some problems.

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Newly discovered molecule could deliver drugs to treat diseases