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June 20, 2026 12 mins
Karsten Eastman, CEO of Sethera Therapeutics whose discovery could be especially useful for enhancing GLP-1 medications such as semaglutide, the active ingredient in Ozempic and Wegovy, which are widely used to treat diabetes and obesity joins eHealth Radio and the Health News Channel. Listen to host Eric Dye & guest Karsten Eastman discuss the following:
  1. For listeners who are not scientists, what exactly was discovered here, and why are researchers excited about it?
  2. What are peptide drugs, and why are they so important in treatments for diabetes and obesity?
  3. What specifically could this discovery do for GLP-1 drugs like semaglutide? Could this eventually mean fewer injections or lower doses for patients?
  4. Could this enzyme technology be used for diseases beyond diabetes and obesity?
  5. How transformative could enzymatic drug engineering become over the next decade, what could medicine look like 10 years from now?
About Karsten Eastman Dr. Karsten Eastman received a PhD from the University of Utah under the mentorship of Professor Vahe Bandarian, where they discovered the key processes that enable Sethera Therapeutics’ innovative technology.

As a co-founder of Sethera, Dr. Eastman is leading the company’s efforts to commercialize cutting-edge peptide therapeutics, drawing on their experience in enzyme and peptide research, patent development, and engagement with key business mentors. About Sethera Therapeutics Founded by University of Utah chemists Vahe Bandarian and Karsten Eastman, Sethera Therapeutics is revolutionizing peptide-based drug development with its enzymatic cross-linking technology. Their platform enables the synthesis of highly stable, polymacrocyclic peptides designed to engage with single targets or multiple targets simultaneously, offering unparalleled precision in therapeutic design. The technology was first developed at the University of Utah with NIH funding and licensed exclusively to Sethera Therapeutics. Website: https://setheratx.com Social Media Links: Linkedin: linkedin.com/company/sethera-therapeutics   X: @SetheraTx  People also listened to this: Natural Curves: A Plastic Surgeon's Guide to Fat Grafting for the Buttocks and Hips with Dr. Noland
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Episode Transcript

Available transcripts are automatically generated. Complete accuracy is not guaranteed.
Speaker 1 (00:00):
This is the eHealth Radio Network, your source for health
advice on demand, and now your host, Eric Michaels.

Speaker 2 (00:07):
Thanks for joining us once again here on the health
radio Network. This is your host, Eric Michaels. E health
Radio gives you the most current health information, news and advice,
featuring some of the leading innovators in healthcare and wellness
who are changing healthcare as we know it. For more
health radio reports, we invite you to visit our main
radio channel site at eHealth radio network dot com. Researchers

(00:29):
have found an enzyme that can turn fragile drug molecules
into durable ring shapes. This could help medications like ozipic
last longer and work more effectively. The process is simpler
and more precise than traditional methods, even for complex drugs.
It may open the door to stronger, longer lasting treatments.

(00:50):
And today we are joined by Carson Eastman. He is
the CEO of Sethera Therapeutics, whose discovery could be especially
useful for enhancing gail medications such as semaglutide. The act
have been greeted in ozipic and we goviy, which are
widely used to treat diabetes and obesity. And miss Reisman,

(01:11):
we thank you for joining us here today.

Speaker 3 (01:12):
Well, thank you so much for having me Eric, that's
great to be here.

Speaker 2 (01:15):
And certainly our pleasure to have you. Thanks so much
for joining us here today. So tell us for starters
for listeners who are not scientists, and that would probably
include most of the audience. What exactly was discovered here
and why are researchers so excited about it?

Speaker 3 (01:30):
Well, what we discovered is a way to use an
enzyme to chemically lock peptides into more stable shapes. This
is important because, as you mentioned, peptides are short chains
of amino acids and they are typically quite fragile. Many
powerful hormones and medicines are peptides, and we're finding a

(01:51):
way to address that challenge of the fragility in the body.
They're typically degraded really quickly, and they often don't hold
natural the exact shape that would be useful for a
strong drug like activity. What our technology does is it
uses these enzymes to install one or more stabilizing cross

(02:13):
links into peptides. I think a really simple way to
think about it is, you know, peptides are like a
flexible string, and we use enzymes to tie it into
very precise loops, and those loops can then make the
molecule more stable, more structured, and generally better suited for
interacting with a biological target. So we and other researchers

(02:35):
are excited about it is this because it allows us
access to peptide structures and architectures that have been difficult
to impossible to make with traditional chemistry alone, and it
allows us to actually explore very large numbers of these
stabilized structures, which not only helps, say the GLP one area,

(02:56):
but also opens new therapeutic possibilities.

Speaker 2 (03:00):
Exciting news and some fantastic information and details on that.
Tell me Also, what are peptide drugs and why are
they so important in treatments for diabetes and obesity? Take
that further if you would.

Speaker 3 (03:12):
That's a great question and the easiest way to think
about it is insulin, which I'm sure everyone knows. Everyone
has someone in their life that's been impacted by diabetes
or has had to take insulin. Insulin is a peptide.
As I mentioned, peptides are made from amino acids, and
they sit in this really important space between small molecule

(03:35):
drugs and large biologics like antibodies. So small molecules are
typically really good at being orally bioavailable, sell penetrant, and
they can address lots of targets, but they have the
downside of being you know, there's some sot off target
and side effects that happen with small molecules. And biologics
are super specific and can be utilized in a lot

(03:59):
of ways, but they have to be injected and they
can't penetrate cells. So peptides can have the best of
both worlds of having the best properties of small molecule
therapeutics and biologics. So in terms of diabetes and obesity,
peptides are especially important because most of the body's natural

(04:21):
signaling hormones are peptides. GLP one is a great example.
It's a peptide hormone that helps regulate insulin secretion, appetite
and has a lot of metabolic control, and drugs like
semic glutide are engineered versions of that biology. The reason
why peptider becomes so important is that they can be
highly highly specific. They can engage with receptors in ways

(04:45):
that small molecules can't actually replicate because small molecules, by
their name, are too small to actually interact and in
the metabolic field, this has been very meaningful for patients
with diabetes and obesity. Big limitation here has been that
linear peptides have very short half lives and typically need

(05:06):
to be stabilized and modified to be able to last longer.
So that's where a lot of new technologies can be
used to improve peptide stability and structure.

Speaker 2 (05:16):
And thanks for your feedback on that. Most helpful. I'm
sure the audience also appreciated you're explaining what are pet
tide drugs? So tell me what specifically could this discovery
do for GLP one drugs like some of glutide. Could
this eventually mean fewer injections or lower doses for patients?

Speaker 3 (05:36):
Bluntly, yes, there's a lot of potential opportunities here. What
we're doing is we have a direct way to improve
the structure, the stability, and even in some cases the
performance of these peptide GLP one receptor agonists. So for
medicine like semaglutide, it's the goal is to not just

(05:57):
make the same molecule in a different way. That's not
what we're trying to do. We're trying to find ways
to make the next generation of peptide structures that have
the same effect on biology, but also have additional improved
properties like lasting longer, difference in tissue exposure, or even
rout of administration. So this could even be not just

(06:18):
fewer injections, but actually oral bioavailability. One of the areas
that is a challenge though, is making it so the
peptide can cross certain barriers, and that's where additional structural
control which our technology enables, helps with. But I'm i
say we have to be very careful here. Ozepic and

(06:39):
we go V are already very highly optimized medicines, and
our view is that this technology can enable the next
generation of peptide therapeutics that can build on the foundation
that they've already established.

Speaker 2 (06:52):
You've got to be excited about this news here today
and really appreciate your visit as well. We're speaking with
Carson Eieseman, THEO Sethera Therapeutics here on Ealth Radio's Health
News channel, part of the Ealth Radio Network. Now, also,
could this enzyme technology be used for diseases beyond diabetes
and obesity?

Speaker 3 (07:12):
Touch on that, yes, and that's one of the areas
that we are most excited about. So we understand that
the gop one drugs are very visible because the public
really understands how impactful they've been with diabetes and obesity.
But peptide therapeutics have much broader potential. These stabilized peptides

(07:35):
can be designed to engage targets in cancer, inflammation, autoimmune diseases,
infectious diseases, and a number of other very difficult to
treat biological pathways. And really this is because peptides sit
in this area, as I mentioned, between small molecules and antibodies.

(07:56):
Small molecules might have too small of say a surface
area to be able to engage the biology in question,
and antibodies are too large and can't penetrate tissue. Stabilize
peptides sit between those two areas. They are large enough
to be able to address these complex biological surfaces, but
they're small and smaller and more tunable than antibodies. The

(08:18):
big implication here is that enzymatically engineered peptides can, and
in my opinion, will, be a great platform for discovering
new medicines against targets that have even been historically difficult
to drug, or targets that have never been drugged before.

Speaker 2 (08:36):
Also, if you win, mister Eastman, how transformative could enzomatic
drug engineering become over the next decade and what could
medicine actually look like, say ten years from now. What's
your thought on that.

Speaker 3 (08:47):
I think that enzymatic drug engineering could really be a
major part of how we create new therapies. Most of
the more recent therapies or therapeutic molecule in many cases
have an enzymatic step somewhere in there in the process.
MERK has actually taken a lot of time to do

(09:09):
additional research and development in this space to make very
highly efficient, highly optimized enzymes to process substrates that will
eventually become therapeutics. What I want to highlight is that
nature already uses enzymes to build very, very complex and
precise molecules, and what we are doing is harnessing that

(09:29):
same logic for drug discovery. Instead of just relying on
synthetic chemistry, which has been fantastic as a building point,
we can use enzymes to access molecules and structures that
otherwise you can't access. So in ten years, I think
that there will be not just more stabilized peptide drugs,

(09:50):
but I think that enzymes will be a critical part
of how small molecules and even biologics are put together.
So I think that we we'll see more durable, more selective,
and easier to use therapeutics for patients. But we also
recognize that there's going to be a lot more data
here because platforms like ours can generate these massive libraries

(10:14):
of novel peptide structures and we can learn what architectures
work best for specific biology.

Speaker 2 (10:22):
Mister Easman, we certainly appreciate this fine report on behalf
of therapeutics, certainly a lot to be excited about. And
if listeners wanted to stay connected to follow any updates,
and or if they had any questions on what you're doing,
where's the best place online to get all the details
and to be connected?

Speaker 3 (10:39):
So we can check us out on our website at
Setherra TX dot com. Search for Sefara on Google will
pop up. You can also follow us on LinkedIn and
those are the best places to check in and any
questions that the listeners might have can also be sent
in through our website. We have a content there and

(11:01):
I'd be happy to answer any that come through.

Speaker 2 (11:03):
Sounds simple enough and again, listeners, you can have access
to that link within the show notes of this broadcast
for your convenience at any time. Mister Eastman, all the
best and thanks for what you do and for joining
us here today.

Speaker 3 (11:16):
Thank you so much for having me, Eric, I appreciate it.

Speaker 2 (11:18):
And certainly our pleasure and honor. Again, we've been speaking
with Carson Eastman, the seof Sathera Therapeutics, who is leading
the company's efforts to commercialize cutting edge peptid therapeutics, drawing
on their experience and enzyme and peptide research, patent development
and engagement with key business mentors. And again for all
the details, visit Sathera TX dot com. And again this

(11:42):
has been your host, Eric Michaels, and we do thank
you for your continue support of the Yealth Radio Network.
Join us again soon for another episode that will help
further expand your knowledge on those things that are important
to your health and wellness. For more Yealth Rate of reports,
we invite you to visit our main radio channel site
at Eelthradio network dot com. And as always we do

(12:03):
thank you for tuning in.

Speaker 1 (12:06):
Thanks for tuning in to the eHealth Radio Network. For
more information or to subscribe to this podcast, visit ehealthradionetwork
dot com,
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