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” I love quotations because it is a joy to find thoughts one might have, beautifully expressed with much authority by someone recognizably wiser than oneself.”

- Marlene Dietrich

Science is Awesome #26

Novel ‘smart’ insulin automatically adjusts blood sugar in diabetic mouse model

February 9, 2015
University of Utah Health Sciences
University of Utah biochemists and fellow scientists have developed a smart insulin that self-activates in response to blood sugar levels. When …

Credit: Matthew Webber

For patients with type 1 diabetes (T1D), the burden of constantly monitoring their blood sugar and judging when and how much insulin to self-inject, is bad enough. Even worse, a miscalculation or lapse in regimen can cause blood sugar levels to rise too high (hyperglycemia), potentially leading to heart disease, blindness and other long-term complications, or to plummet too low (hypoglycemia), which in the worst cases can result in coma or even death.

To mitigate the dangers inherent to insulin dosing, a University of Utah biochemist and fellow scientists have created Ins-PBA-F, a long-lasting “smart” insulin that self-activates when blood sugar soars. Tests on mouse models for type 1 diabetes show that one injection works for a minimum of 14 hours, during which time it can repeatedly and automatically lower blood sugar levels after mice are given amounts of sugar comparable to what they would consume at mealtime.

Ins-PBA-F, acts more quickly, and is better at lowering blood sugar, than long-acting insulin detimir, marketed as LEVIMIR. In fact, the speed and kinetics of touching down to safe blood glucose levels are identical in diabetic mouse models treated with Ins-PBA-F and in healthy mice whose blood sugar is regulated by their own insulin. A study showing these findings will be published Feb. 9 in PNAS Early Edition.

“This is an important advance in insulin therapy,” says co-first author Danny Chou, Ph.D., USTAR investigator and assistant professor of biochemistry at the University of Utah. “Our insulin derivative appears to control blood sugar better than anything that is available to diabetes patients right now.” He will continue evaluating the long-term safety and efficacy of Ins-PBA-F. The insulin derivative could reach Phase 1 human clinical trials in two to five years.

“At present, there is no clinically approved glucose-responsive modified insulin,” says Matthew Weber, Ph.D., co-first author with Chou and Benjamin Tang, Ph.D., who performed the work together while postdoctoral fellows at MIT in collaboration with senior authors and MIT professors Robert Langer, Ph.D., and Daniel Anderson, Ph.D. “The development of such an approach could contribute to greater therapeutic autonomy for diabetic patients.”

The hallmark symptom of diabetes is inadequate control of blood sugar. The deficit is most pronounced in type 1 diabetes, which develops when insulin-producing beta-cells of the pancreas are destroyed. Without insulin, there is no way to shuttle sugar out of the blood and into cells, where it is used for energy. T1D patients depend on daily insulin injections for survival.

Despite advances in diabetes treatment such as insulin pumps and the development of four types of insulin, patients must still manually adjust how much insulin they take on a given day. Blood sugar levels vacillate widely depending on a number of factors such as what someone chooses to eat and whether they exercise.

A glucose-responsive insulin that is automatically activated when blood sugar levels are high would eliminate the need for additional boosts of insulin, and reduce the dangers that come with inaccurate dosing. Various such “smart” insulins under development typically incorporate a protein-based barrier, such as a gel or coating, that inhibits insulin when blood sugar is low. However, such biologically based components are often sources of trouble, provoking unwanted side effects such as an immune response.

Ins-PBA-F differs in that it was created by chemically modifying insulin directly. Ins-PBA-F consists of a long-acting insulin derivative that has a chemical moiety, phenylboronic acid (PBA), added to one end. Under normal conditions, Ins-PBA-F binds to serum proteins that circulate in the bloodstream, blocking its activity. When blood sugar levels are high, glucose sugars bind PBA, which acts like a trigger to release Ins-PBA-F so it can get to work.

“Before, a ‘smart’ insulin really meant delivering insulin differently,” says Chou. “Ins-PBA-F fits the true definition of ‘smart’ insulin, where the insulin itself is glucose responsive. It is the first in its class.”

Chou explains that because Ins-PBA-F is a chemically modified version of a naturally occurring hormone, he thinks it is likely to be safe enough to use on a daily basis, similar to other insulin derivatives that are on the market today.

“My goal is to make life easier, and safer for diabetics,” he says.

This work was supported by the Leona M. and Harry B. Helmsley Charitable Trust, the Tayebati Family Foundation, the National Institutes of Health, and the Juvenile Diabetes Research Foundation.

Story Source:

The above story is based on materials provided by University of Utah Health SciencesNote: Materials may be edited for content and length.

Journal Reference:

  1. Danny Hung-Chieh Chou, Matthew J. Webber, Benjamin C. Tang, Amy B. Lin, Lavanya S. Thapa, David Deng, Jonathan V. Truong, Abel B. Cortinas, Robert Langer, Daniel G. Anderson. Glucose-responsive insulin activity by covalent modification with aliphatic phenylboronic acid conjugatesProceedings of the National Academy of Sciences, 2015; 201424684 DOI:10.1073/pnas.1424684112

Cite This Page:

University of Utah Health Sciences. “Novel ‘smart’ insulin automatically adjusts blood sugar in diabetic mouse model.” ScienceDaily. ScienceDaily, 9 February 2015. <www.sciencedaily.com/releases/2015/02/150209161141.htm>.

SEO Tips, Insights, and other News #2


How Long Does SEO Take To Start Working?

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Science is Awesome #25

15-million-year-old mollusk protein found

February 5, 2015
Carnegie Institution
A 15-million year old fossil gastropod, Ecphora, from the Calvert Cliffs of southern Maryland is depicted. The golden brown color arises from the original shell-binding proteins and pigments preserved in the mineralized shell.
Credit: John Nance

A team of Carnegie scientists have found “beautifully preserved” 15 million-year-old thin protein sheets in fossil shells from southern Maryland. Their findings are published in the inaugural issue of Geochemical Perspectives Letters.

The team–John Nance, John Armstrong, George Cody, Marilyn Fogel, and Robert Hazen–collected samples from Calvert Cliffs, along the shoreline of the Chesapeake Bay, a popular fossil collecting area. They found fossilized shells of a snail-like mollusk called Ecphora that lived in the mid-Miocene era–between 8 and 18 million years ago.

Ecphora is known for an unusual reddish-brown shell color, making it one of the most distinctive North American mollusks of its era. This coloration is preserved in fossilized remains, unlike the fossilized shells of many other fossilized mollusks from the Calvert Cliffs region, which have turned chalky white over the millions of years since they housed living creatures.

Shells are made from crystalline compounds of calcium carbonate interleaved with an organic matrix of proteins and sugars proteins and sugars. These proteins are called shell-binding proteins by scientists, because they help hold the components of the shell together.They also contain pigments, such as those responsible for the reddish-brown appearance of the Ecphora shell. These pigments can bind to proteins to form a pigment-protein complex.

The fact that the coloration of fossilized Ecphora shells is so well preserved suggested to the research team that shell proteins bound to these pigments in a complex might also be preserved. They were amazed to find that the shells, once dissolved in dilute acid, released intact thin sheets of shell proteins more than a centimeter across. Chemical analysis including spectroscopy and electron microscopy of these sheets revealed that they are indeed shell proteins that were preserved for up to 15 million years.

“These are some of the oldest and best-preserved examples of a protein ever observed in a fossil shell,” Hazen said.

Remarkably, the proteins share characteristics with modern mollusk shell proteins. They both produce thin, flexible sheets of residue that’s the same color as the original shell after being dissolved in acid. Of the 11 amino acids found in the resulting residue, aspartate and glutamate are prominent, which is typical of modern shell proteins. Further study of these proteins could be used for genetic analysis to trace the evolution of mollusks through the ages, as well as potentially to learn about the ecology of the Chesapeake Bay during the era in which Ecphora thrived.

Story Source:

The above story is based on materials provided by Carnegie InstitutionNote: Materials may be edited for content and length.


SEO Tips, Insights, and other News #1


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