D2 Digital by Design: service delivery innovation award runner-up

Service users are sent personalised messages of support by the Response Prevention Project team. Photograph: Jason Lock/Jason Lock Photography

Text messages that support people recovering from alcohol misuse has significantly cut the number of people who relapse and have to be referred back to services.

Daily personalised support messages – which prompt a service user who has recently completed an alcohol misuse programme to reflect on their recovery – are delivered automatically as part of the Bolton Response Prevention Project called Shine.

The questions take into account the user's triggers to drink, such as the time of day they are likely to crave alcohol and also what motivates them to stop drinking such as their relationships with their family.

Service users are also asked whether they feel OK, or are struggling and need more support, and are sent appropriate messages.

Project manager Renate Kalnina at digital technology company D2 Digital by Design in Manchester, which is behind the initiative, says: "If they respond 'OK' we send them back a congratulatory message; if they are 'struggling' then the personalised intervention messages come into play.

"If they say that they need more support then the services get notified within 15 minutes and they get in touch with the client."

Service users are also sent a reminder via text message for appointments as part of the project, which ran from April 2010 to December 2012 in partnership with alcohol misuse services in Bolton.

Only 2.2% of Shine service users had to be re-referred for treatment, compared to 9.5% of non-Shine service users; a significant" reduction according to an analysis of the project.

Clients' attendance rates for relapse prevention programmes improved – rising from 42% to 72% in tier three services (medical intervention and psychosocial support) and from 17% to 72% in tier two services, which offer less intensive support and aftercare, the analysis revealed.

It is estimated the initiative has saved between £68,260 and £399,150, depending on individual client need.

D2 Digital by Design is in discussion with Public Health England about using the same model to support opiate users.

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New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals

Main Category: Biology / Biochemistry
Also Included In: Pharma Industry / Biotech Industry
Article Date: 30 Jul 2013 - 0:00 PDT Current ratings for:
New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals

Just 12 molecules of water cause the long post-activation recovery period required by potassium ion channels before they can function again. Using molecular simulations that modeled a potassium channel and its immediate cellular environment, atom for atom, University of Chicago scientists have revealed this new mechanism in the function of a nearly universal biological structure, with implications ranging from fundamental biology to the design of pharmaceuticals. Their findings were published online in Nature.

"Our research clarifies the nature of this previously mysterious inactivation state. This gives us better understanding of fundamental biology and should improve the rational design of drugs, which often target the inactivated state of channels" said Benoît Roux, PhD, professor of biochemistry and molecular biology at the University of Chicago.

Potassium channels, present in the cells of virtually living organisms, are core components in bioelectricity generation and cellular communication. Required for functions such as neural firing and muscle contraction, they serve as common targets in pharmaceutical development.

These proteins act as a gated tunnel through the cell membrane, controlling the flow of small ions into and out of cells. After being activated by an external signal, potassium channels open to allow ions through. Soon after, however, they close, entering an inactive state and are unable to respond to stimuli for 10 to up to 20 seconds.

The cause of this long recovery period, which is enormously slow by molecular standards, has remained a mystery, as structural changes in the protein are known to be almost negligible between the active and inactivated states - differing by a distance equivalent to the diameter of a single carbon atom.

To shed light on this phenomenon, Roux and his team used supercomputers to simulate the movement and behavior of every individual atom in the potassium channel and its immediate environment. After computations corresponding to millions of core-hours, the team discovered that just 12 water molecules were responsible for the slow recovery of these channels.

They found that when the potassium channel is open, water molecules quickly bind to tiny cavities within the protein structure, where they block the channel in a state that prevents the passage of ions. The water molecules are released slowly only after the external stimulus has been removed, allowing the channel to be ready for activation again. This computer simulation-based finding was then confirmed through osmolarity experiments in the laboratory.

"Observing this was a complete surprise, but it made a lot of sense in retrospect," Roux said. "Better understanding of this ubiquitous biological system will change how people think about inactivation and recovery of these channels, and has the potential to someday impact human health."

Article adapted by Medical News Today from original press release. Click 'references' tab above for source.
Visit our biology / biochemistry section for the latest news on this subject.

The work was supported by grants from the National Institutes of Health. Computation resources were provided by Oak Ridge National Laboratory, the National Resource for Biomedical Supercomputing and the Pittsburgh Supercomputing Center.

University of Chicago Medical Center

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http://www.medicalnewstoday.com/releases/264056.php.

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'New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals'

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View the original article here

New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals

Main Category: Biology / Biochemistry
Also Included In: Pharma Industry / Biotech Industry
Article Date: 30 Jul 2013 - 0:00 PDT Current ratings for:
New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals

Just 12 molecules of water cause the long post-activation recovery period required by potassium ion channels before they can function again. Using molecular simulations that modeled a potassium channel and its immediate cellular environment, atom for atom, University of Chicago scientists have revealed this new mechanism in the function of a nearly universal biological structure, with implications ranging from fundamental biology to the design of pharmaceuticals. Their findings were published online in Nature.

"Our research clarifies the nature of this previously mysterious inactivation state. This gives us better understanding of fundamental biology and should improve the rational design of drugs, which often target the inactivated state of channels" said Benoît Roux, PhD, professor of biochemistry and molecular biology at the University of Chicago.

Potassium channels, present in the cells of virtually living organisms, are core components in bioelectricity generation and cellular communication. Required for functions such as neural firing and muscle contraction, they serve as common targets in pharmaceutical development.

These proteins act as a gated tunnel through the cell membrane, controlling the flow of small ions into and out of cells. After being activated by an external signal, potassium channels open to allow ions through. Soon after, however, they close, entering an inactive state and are unable to respond to stimuli for 10 to up to 20 seconds.

The cause of this long recovery period, which is enormously slow by molecular standards, has remained a mystery, as structural changes in the protein are known to be almost negligible between the active and inactivated states - differing by a distance equivalent to the diameter of a single carbon atom.

To shed light on this phenomenon, Roux and his team used supercomputers to simulate the movement and behavior of every individual atom in the potassium channel and its immediate environment. After computations corresponding to millions of core-hours, the team discovered that just 12 water molecules were responsible for the slow recovery of these channels.

They found that when the potassium channel is open, water molecules quickly bind to tiny cavities within the protein structure, where they block the channel in a state that prevents the passage of ions. The water molecules are released slowly only after the external stimulus has been removed, allowing the channel to be ready for activation again. This computer simulation-based finding was then confirmed through osmolarity experiments in the laboratory.

"Observing this was a complete surprise, but it made a lot of sense in retrospect," Roux said. "Better understanding of this ubiquitous biological system will change how people think about inactivation and recovery of these channels, and has the potential to someday impact human health."

Article adapted by Medical News Today from original press release. Click 'references' tab above for source.
Visit our biology / biochemistry section for the latest news on this subject.

The work was supported by grants from the National Institutes of Health. Computation resources were provided by Oak Ridge National Laboratory, the National Resource for Biomedical Supercomputing and the Pittsburgh Supercomputing Center.

University of Chicago Medical Center

Please use one of the following formats to cite this article in your essay, paper or report:

MLA

University of Chicago Medical Center. "New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals." Medical News Today. MediLexicon, Intl., 30 Jul. 2013. Web.
30 Jul. 2013. APA
University of Chicago Medical Center. (2013, July 30). "New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals." Medical News Today. Retrieved from
http://www.medicalnewstoday.com/releases/264056.php.

Please note: If no author information is provided, the source is cited instead.

'New mechanism in the function of a nearly universal biological structure will impact fundamental biology, design of pharmaceuticals'

Please note that we publish your name, but we do not publish your email address. It is only used to let you know when your message is published. We do not use it for any other purpose. Please see our privacy policy for more information.

If you write about specific medications or operations, please do not name health care professionals by name.

All opinions are moderated before being included (to stop spam). We reserve the right to amend opinions where we deem necessary.

Contact Our News Editors

For any corrections of factual information, or to contact the editors please use our feedback form.

Please send any medical news or health news press releases to:

Note: Any medical information published on this website is not intended as a substitute for informed medical advice and you should not take any action before consulting with a health care professional. For more information, please read our terms and conditions.

View the original article here