Protein Aggregation: The Black Coffee of Drug Discovery

By Scott Wallask

Conference Producer, IBC Life Sciences

I don’t drink coffee. I have had less than 10 cups in my entire life, and the last one I sampled was so terrible I dumped it down a storm drain in the street.

Part of my reason for not liking coffee is there are too many choices. Years ago, my wife’s parents – who are big coffee drinkers – took a road trip to visit us and asked that we grab them some coffee for their stay.

My wife and I asked what kind of coffee they wanted, and we got the good old response, “Oh, any kind is fine.”

My wife doesn’t drink coffee, either (so much for opposites attracting), so my in-laws were quite disappointed when they arrived to find instant coffee waiting for them. My wife and I had no idea what we were buying.

So I sympathize with protein researchers who may sense trouble brewing when they have to choose among a varied selection of instruments and technologies designed to analyze aggregation levels in their drug products.

Protein aggregation seems like black coffee to me: It’s not sweet and you’ve got to be tough to handle it. But minimizing protein aggregation is an effort taking place throughout the drug discovery pipeline, from early research through formulation, all the way to the patient. Technology is a valuable aid when you’re doing aggregation-themed work on the molecular level.

So I’m happy to see so much interest in our technology sessions at IBC’s upcoming Protein Aggregation, Stability & Solubility conference, which takes place June 4-6, 2014, in downtown San Francisco.

One of the highlights of the program for me is a panel discussion with a simple mission: Explore the pros and cons of various tools used to measure aggregation. Our panelists will likely hit upon field-flow fractionation, fluorescence spectroscopy, chromatography, transmission electron microscopy, light-scattering techniques, and ultra-centrifugation — along with any other technologies our audience asks about.

The event also features the following individual presentations about analytical and particle characterization technologies:

• ·  Protein Aggregation and Emerging Tools to Support Development and Characterization (presenter from Gilead Sciences, Inc.)
• ·  New Orthogonal Methods to Test Biopharmaceutical Solutions for the Presence of Aggregates and Particulate Matter (University of Geneva)
• ·  Methods for the Characterization of Biotherapeutic Aggregates (Pfizer, Inc.)
• ·  Light-Scattering Toolbox for Predicting and Characterizing Aggregation (Wyatt Technology Group)
• ·  Use of Solution Nuclear Magnetic Resonance to Identify Site-Specific Structural Changes in Proteins that Precede Aggregation (University of Kansas)

We’d love to see you at the conference, which is the one largest ever dedicated to protein aggregation concerns.

P.S. If you find a coffee flavor you think I’ll like, swing by registration at the event and let me know.

You can find more information on the Protein Aggregation, Stability & Solubility conference here. Register now and save 20%. Use discount code D14200BLOG.

Follow Scott on Twitter @Scott_biopharma

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Naked Mole Rats and Fighting Degenerative Disease

This post was authored by @MikeMadarasz of the Institute for International Research

Did you know that the naked mole rat holds the record for the longest living rodent?  It’s a nice piece of trivia, yes, but the longevity of this animal may actually provide us clues about fighting degenerative diseases such as Alzheimers and Parkinsons.  Naked mole rats have been known to live for as long as 31 years—an incredible age based on their size.  In comparison, mice live four years at the most.  This is something that has piqued the interest of scientists for years.

A recent study from the University of Texas Health Science Center in San Antonio has made connections between the extended lifespan of these rodents and the chaperone protein HSP25.  HSP25, as well as other chaperone proteins, serve as a sort of protein audit team by quickly eliminating those that are incorrectly produced or defective.  These flawed proteins are capable of aggregating and forming “clumps”, which have been associated with degenerative diseases.  

Recently, researchers have been able to definitively correlate the presence of HSP25 in tissue with longevity.  Says Karl Rodriguez, Ph.D., a postdoctoral fellow at the University of Texas Health Science, "If we can understand how HSP25 levels are regulated, what it’s function is and how it contributes to cell health, we might find ways to use this protein to combat devastating age-related diseases."  Rodriguez cites animals with higher levels HSP25 as being more “primed to react” to faulty proteins and in turn, maintain cell health.  Finding ways to increase the human equivalent of the HSP25 protein (HSP27) could potentially help prevent these diseases.

Said Rochelle Buffenstein, Ph.D, the study’s senior investigator, "There's still a lot we can learn from extremely long-lived animals. Use of such models enables us to evaluate whether nature—through millions of years of evolutionary experimentation—has already evolved the best way to maintain cellular integrity and thereby delay and attenuate the aging process. HSP25 may be one such evolved protein."

Read the full press release here.

Get more on the latest in protein research at IIR’s Protein Aggregation, Stability & Solubility conference, June 4-6 in San Francisco. Learn more here.

Register now and SAVE 20%. Use code D14200BLOG

BEST VALUE. Get three conferences for the price of one. Check out our all access passes to Bioconjugates: From Targets to Therapeutics and the Next Generation Protein Summit.  

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