Chemistry

Alzheimer's disease

Alzheimer's disease


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Area of ​​Expertise - medicine

Alzheimer's disease is a neurodegenerative disease which, in addition to various neurological abnormalities, is symptomatically characterized by changes in behavior, reduced memory performance and a progressive loss of cognitive abilities. It is therefore one of the dementia diseases. It is named after the German psychiatrist Alois Alzheimer, who first described the histopathological changes in brain tissue at the beginning of the 20th century. In the western industrialized countries, about 70% of all dementia cases are attributed to Alzheimer's disease. An exact diagnosis can only be made by microscopic examination of the brain tissue after the patient's death. In medical practice, psychological and neurological tests are therefore used to make a diagnosis.

In patients with Alzheimer's disease, typical protein deposits, the so-called amyloid plaques, which are also known as senile plaques, are found in the brain. They consist of the protein β-amyloid, which, unlike in healthy humans, accumulates in large quantities and is deposited on blood vessels and neurons of the brain. Although the exact molecular mechanisms in the development of Alzheimer's disease have not yet been clarified, a widely accepted hypothesis assumes that these deposits eventually lead to the death of neurons and thus cause the symptoms of dementia.

Learning units in which the term is dealt with

Nervous system diseases60 min.

BiochemistryMedicinal chemistry and biochemistryPathobiochemistry

Important representatives of neurotoxins, some ion channel diseases, as well as Parkinson's syndrome and Alzheimer's disease are presented.


Inhibition of the enzyme meprin-β, which is involved in the development of Alzheimer's disease, analyzed

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Researchers at Johannes Gutenberg University Mainz and the Institute of Molecular Biology of Barcelona have found out how the blood plasma protein fetuin-B binds to the enzyme meprin-β and visualized their findings with a computer model. These results could lead to the development of drugs for serious diseases such as Alzheimer's and cancer.

Research results from JGU could lead to the development of new drugs

Researchers at Johannes Gutenberg University Mainz (JGU) and the Institute of Molecular Biology of Barcelona have found out how the blood plasma protein fetuin-B binds to the enzyme meprin-β and visualized their findings with a computer model. These results could lead to the development of drugs to treat serious diseases such as Alzheimer's and cancer. In humans, Meprin-β releases proteins from cell surfaces and thereby controls important body functions. However, a dysregulation of this process can cause the diseases mentioned. Meprin-β is regulated by fetuin-B, because it binds to the enzyme if necessary and thus prevents the release of other proteins. In the journal Proceedings of the National Academy of Sciences, the researchers are the first to describe this bond in detail.

The JGU scientists produced both meprin-β and fetuin-B in insect cells and allowed them to react with one another in a test tube. Using enzyme kinetic measurements and biophysical analyzes, they determined that this reaction had resulted in an extremely stable, high-molecular complex. Her colleagues in Barcelona then succeeded in crystallizing the complex and clarifying its three-dimensional structure by means of an X-ray crystal structure analysis. The protein crystals were bombarded with X-rays and the atomic structure of the crystals was calculated from the diffraction of the X-rays. The structure was then illustrated with a computer model. “Using the model, we can now see exactly how meprin-β and fetuin-B bind to one another,” says Prof. Dr. Walter Stöcker, who with Dr. Hagen Körschgen and Nele von Wiegen participated in the research on the part of JGU. “We have thus created an excellent starting point for a better understanding of diseases such as Alzheimer's disease and for the development of drugs against it.” It is already known that meprin-β is involved in the formation of the so-called beta-amyloid plaques, which are characteristic of the Disease are. It has also been observed that people with Alzheimer's have relatively little fetuin-B in their blood, and that this may lead to poor control of meprin-β. "If it is possible to develop a drug that, like fetuin-B, binds to the enzyme and thereby inhibits it, this could represent a new way of treating Alzheimer's," says Stöcker.


Challenge

The sporadic form of Alzheimer's disease (AD) is the most common form accounting for 90-95% of cases. Surprisingly, there is no animal model for sporadic AD available on the market. AD mouse models generally express mutant amyloid precursor protein (APP), which liberates amyloid beta peptides. The latter are the toxic agents in AD. It is well established however that precursor APP overexpression causes a plethora of unwanted effects. APP has an established growth factor function competing with the pathological effect of Abeta.


Alzheimer's Disease - Chemistry and Physics

An early diagnosis of Alzheimer's disease has many advantages: Treatment can start early and thus maintain quality of life. In addition, people who were diagnosed at an early stage can still take care of important things on their own and make provisions for the future. Up to now, early diagnosis with the diagnostic methods currently available has been laborious and does not always lead to a clear result. Dr. Maria Cramm from the University Medical Center Göttingen would like to change this.

To this end, she tries to make the “Real-Time Quaking Induced Conversion” (RT-QuIC), which is used to diagnose prion diseases such as Creutzfeldt-Jakob disease, also applicable to the diagnosis of Alzheimer's disease. Misfolded proteins play a central role in both prion diseases and Alzheimer's disease. The two-year research project is funded by the non-profit Alzheimer Research Initiative e.V. (AFI) with 40,000 euros.

“With the RT-QuIC method, misfolded proteins can be reproduced so that even the smallest amounts of protein can be measured. In the case of prion diseases, the method delivers very precise results. If the RT-QuIC method also proves to be reliable in diagnosing Alzheimer's disease, the disease could be detected earlier with certainty, ”says Dr. Maria Cramm.

Dr. Cramm and her team will initially modify the RT-QuIC method for use in Alzheimer's diagnosis. The aggregation behavior of the proteins beta-amyloid and tau typical for Alzheimer's disease is shown. This is followed by a comparison with known biomarkers that are at the center of current Alzheimer's diagnosis.

AFI is the largest private sponsor of Alzheimer's research at German universities and public institutions. The AFI can currently support ten new research projects with a total of 798,357 euros. So far, a total of 230 research activities by committed scientists have been financed with over 9.2 million euros.

The projects worthy of funding were selected by the AFI Scientific Advisory Board chaired by Prof. Thomas Arendt (University of Leipzig) together with the advisory boards of the international cooperation partners Alzheimer Nederland in the Netherlands and Fondation Vaincre Alzheimer in France as well as external experts in peer review. Funding is provided for projects in the areas of basic, cause, diagnosis, prevention and drug research at the university locations in Bonn, Coburg, Düsseldorf, Göttingen, Heidelberg, Leipzig, Saarbrücken and Ulm.

About the Alzheimer Research Initiative e.V.
The Alzheimer Research Initiative e.V. (AFI) is a registered non-profit association. Since 1995, AFI has been using donations to support research projects by committed Alzheimer's researchers and has made information material available to the public free of charge. To date, AFI has supported 230 research activities with over 9.2 million euros and distributed around 800,000 guides and brochures. Interested parties and those affected can find detailed information about Alzheimer's disease at www.alzheimer-forschung.de and request educational material. Information on the work of the association and all donation options can also be found on the website. The AFI ambassador is the journalist and sports presenter Okka Gundel.

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Features of this press release:
Journalists, scientists, everyone
Biology, chemistry, nutrition / health / care, medicine
supraregional
Research projects
German


Health Benefits of Pet Therapy

Pet therapy means the use of cats, dogs, or other animals to create a health benefit to its human companion. Studies have proven that pet therapy is effective in helping people feel physically and mentally. As long as an appropriate animal is used, pet therapy is an excellent additional treatment.

Description

The Utah Animal Assisted Therapy Association defines pet therapy as the use of animals to promote health and healing. This therapy can be used with individuals of all ages, from children to the elderly, and the benefits can be physical, mental, and emotional (see Resources).

Physical benefits

According to the naturopathic healthspring.net website, studies have shown that petting animals can bring down a person's blood pressure and trigger the release of dopamine and serotonin in the brain that can lift a person's mood. Children who were hospitalized with pets through therapy experienced less pain (see Resources).

Psychological benefits

Healthspring.net says that in the health sector with high pressure orders, animals benefit from reduced stress from close therapy. Studies have also shown that animal therapy can help patients with dementia and Alzheimer's disease.

Types

Although dogs and cats are the animals most commonly used in pet therapy, a variety of other animals can be used with positive results. Fish in an aquarium can lower stress levels, and birds can be effective too. Horses and dolphins are used for pet therapy for autistic children.

Requirement

There are no official requirements for pets used for therapy. The Utah Animal Assisted Therapy Association recommends that animals be calm, well trained, and very social.


Alzheimer's - 4th version - lecture

Disguise:
What is Alzheimer's?
How common is this disease?
What Causes Alzheimer's Disease?
What happens in the brain in Alzheimer's disease?
How does Alzheimer's disease work?
How is Alzheimer's disease diagnosed?
Diagnosis of Alzheimer's disease - what drugs are there?
Diagnosis of Alzheimer's disease - what other therapy options are there?
Diagnosis of Alzheimer's disease - what can I do (as a relative)?
Can you prevent Alzheimer's disease?

What is Alzheimer's?
Alzheimer's disease
Named after Alois Alzheimer (1864-1915), German neurologist
Progressive shrinkage of the brain (often due to multifactorial inheritance)

How common is this disease?
AT THIS POINT, I JUST LOOKED FOR A GRAPHIC FROM THE INTERNET

What Are the Causes of Alzheimer's Disease?
- Involvement of several factors:
Age
Damage to the brain: - Circulatory disorders d. Brain (e.g. from a stroke) is not a cause
-Damages can cause the symptoms to appear earlier
Inheritance: - rare case to get sick (approx. 1% - 5%)

What happens in the brain in Alzheimer's disease?
AT THIS POINT I HAVE PRESENTED A VERY INFORMATIVE VIDEO. I DON'T KNOW EXACTLY WHAT IT'S called.

How does Alzheimer's disease work?
slowly progressive brain disease lasting 5 to 20 years
three different stages:
- Early stage: - almost imperceptible onset (symptoms barely noticeable)
-easy forgetfulness (e.g. familiar terms / names)
- increasing difficulty of complicated tasks
- usual actions fail (e.g. tying shoes)
-Everyday life can be mastered with just a few problems

The middle phase: -obvious symptoms
- severe impairment of memory
-Mixing past and present
- Difficult to understand language makes communication difficult
Orientation disorders (even in your own household)
- delusions
- delusions
-Rependent on support for everyday tasks, such as personal hygiene
-Control of the bowel and bladder is decreasing

The third stage: -Help needed in all areas of life
- Limited language except for a few words
-Memory totally fails
-Eating and drinking only possible with help

- sluggish and unsteady gait
- complete loss of orientation
- Seizures and swallowing disorders
- Bedridden sick people are at risk of infection
-Many eventually die of pneumonia


How is Alzheimer's disease diagnosed?
Warning signs: -forgetting recent events
-social withdrawal (e.g. silence in larger groups)
-decreasing interest in work, hobbies and contacts
anamnese
Laboratory tests: -Blood and urine tests
-Lumbar puncture
Imaging procedures: -CT / MRI
-Ultrasonic examination
EKG / EEG

Diagnosis of Alzheimer's disease - what drugs are there?
Antidementia drugs: - Nerve cells die
-cannot be prevented until today, but by taking antidementia drugs the progressive symptoms can be slowed down, gain in time and quality of life

Diagnosis of Alzheimer's disease - what other therapies are there?
Cognitive training: -playful learning with reference to everyday life
-Simultaneous use of several sensory channels
-If only the Alzheimer's symptoms are trained (e.g. memory), it can lead to excessive demands
-Only useful for the early stage
Family work: - Difficult tasks cannot be mastered alone in the long run
- Relief very important
(-Multiprofessional team of the memory consultation in the university clinic available)

Alzheimer's diagnosis - what can I do (as a relative)?
- clarify open questions (with doctors / nurses)
-Use the knowledge of experts
- timely provision
- Thoroughly inform
- Ensure the safety of the sick
-Maintain communication
- Be able to respond to mood swings

Can you prevent Alzheimer's disease?
- physical and mental activity
-Fish and seafood


Nobel Prize in Chemistry: Two Americans and a Briton share an award

Nobel Prize in Chemistry goes to a researcher and two researchers

With the results of the investigations in the field of so-called & # 034Directed evolution & # 034, a wide variety of products can be manufactured: from bio-fuels to pharmaceuticals.

Their methods help patients and open up new avenues: These six researchers are delighted with one of the world's most prestigious awards.

Stockholm / Berlin. With evolution as a model, three protein researchers have created opportunities for more environmentally friendly production of pharmaceuticals and biofuels - and have now received the Nobel Prize in Chemistry for this. Half of the award, endowed with around 870,000 euros (9 million Swedish crowns), goes to the American Frances Arnold (62) and the other half to her compatriot George Smith (77) and the British Gregory Winter (67), like the Royal -Swedish Academy of Sciences announced in Stockholm on Wednesday.

The three researchers have succeeded in controlling evolution and using it for purposes that have brought mankind the greatest benefit. The Nobel Committee calls the American Frances Arnold, fifth Nobel Prize winner in chemistry to date, the “star of enzyme engineering”, who now works at the California Institute of Technology in Pasadena.

Frances went into research - executive posts would have been too much work

She actually wanted to become a diplomat or CEO of a multinational company. But then the US scientist Frances Arnold decided to research renewable energies because a managerial position would have meant too much work, she said a few months ago.

Their method can be used to optimize molecules such as proteins or DNA. Tailor-made enzymes are used, for example, to produce pharmaceuticals or biofuels - which are often more environmentally friendly than before, as the Nobel Committee emphasizes.

Antibodies against athritis, tumors and Alzheimer's

George Smith developed a method in which so-called bacteriophages - viruses that infect bacteria - are used to create new proteins. Gregory Winter at Cambridge used this process, known as phage display, to develop antibodies for specific purposes. “This achievement was the starting point for a pharmaceutical revolution,” writes the Nobel Committee.

The human antibody adalimumab, which is used against rheumatoid arthritis, among other things, emerged from the work. Antibodies are also used in tumor therapy or researched for the treatment of Alzheimer's disease.

The 67-year-old will head Trinity College in Cambridge until next summer - the facility is considered a forge for Nobel Prize winners. The college has produced more than 30 personalities who have received the high distinction - including in other areas such as literature and peace.

Laser tweezers for holding viruses and cells

On Tuesday, three laser experts were awarded the Nobel Prize in Physics for developing high-precision tools made from light. Half of the award goes to the American Arthur Ashkin (96). The French Gérard Mourou (74) and the Canadian Donna Strickland (59) share the second half.

Millions of patients worldwide benefit from the invention that Mourou and Strickland developed together. The best known is probably the ablation of the cornea by laser, which is carried out millions of times worldwide. The Nobel Committee emphasizes that new drugs, more efficient solar cells or better catalysts could also be produced in the future.

Until the researchers' developments, it was considered science fiction to use the power of light. In the US series “Star Trek”, for example, the spaceship has a tractor beam with which objects can be held and moved. The optical tweezers developed by Ashkin come at least close to this idea: they can be used to hold and move individual bacteria, viruses and living cells with laser beams. Such laser tweezers are now used in a number of laboratories.

Oldest Nobel Prize Winner ever

At 96 years of age, the oldest Nobel Prize winner to date reacted calmly to the award. Ashkin told the Nobel Committee that he could not give interviews and that he was very busy with a recent publication.

Strickland reacted more exuberantly to the call from Stockholm: “First you have to think: This is crazy.” Strickland is only the third winner of the Nobel Prize in Physics - 55 years after Maria Goeppert Mayer (1963). Marie Curie had received a Nobel Prize in Physics in 1903. "We have to celebrate women physicists because they are out there," said Strickland. "I am honored to be one of these women."

Immunotherapy against cancer

The winners in medicine were announced on Monday: The American James Allison and the Japanese Tasuku Honjo received the lavish award for the development of immunotherapies against cancer. The ceremonial presentation of the Nobel Prizes traditionally takes place on December 10th, the anniversary of the death of the prize donor Alfred Nobel. (dpa)


Near-Infrared Photoactivatable Oxygenation Catalysts of Amyloid Peptide

A new, biocompatible photooxygenation catalyst that can selectively oxidize and degrade the pathogenic aggregation of Alzheimer's disease (AD) -related amyloid-β-peptide (Aβ) under near-infrared (NIR) light irradiation has been developed. The catalyst was able to oxygenate Aβ, which was embedded under the skin of a living mouse, and reduced the intact Aβ level in the AD model mouse brain. The new catalyst has potential for the treatment of peripheral amyloid diseases and AD.

The toxic aggregation of amyloid peptide and protein is closely linked to a number of human diseases. Amyloid-β (Aβ) is a representative amyloid peptide whose aggregation is related to the pathogenesis of Alzheimer's disease (AD). The development of an artificial chemical system that selectively converts toxic amyloid aggregates into non-toxic species under physiological conditions, possibly suppressing the pathogenic process, could be a new therapeutic strategy for the treatment of currently incurable amyloid diseases, including AD.

The researchers envisioned that photocatalytic aerobic oxygenation would be a suitable chemical reaction to attenuate the pathogenic aggregation properties of Aβ under physiological conditions. Since peptide and protein aggregation generally depends on intermolecular hydrophobic interactions, the covalent introduction of hydrophilic oxygen atoms into a peptide or protein (ie oxygenation) would reduce the aggregation property. We previously reported that aerobic oxygenation of Aβ occurs in the presence of flavin (vitamin B2) based photocatalysts, and the resulting oxygenated Aβ shows very low aggregation ability and toxicity. Thereafter, more selective photooxygenation catalysts, which are only activated when a toxic higher order amyloid structure is detected, based on a fluorescent probe for aggregated amyloid peptide and protein. However, the in vivo use of the catalysts was not feasible because irradiation with visible light, which has low tissue penetration, was necessary for the catalyst to be excited. For in vivo use, photocatalysts must be able to work with longer-wave light when excited, which is referred to as an "optical window" in which living tissue absorbs relatively little light.

Here we developed a biocompatible photooxygenation catalyst that can selectively oxidize and degrade the pathogenic aggregation of Aβ under irradiation with near infrared (NIR). The catalyst demonstrated four main advantages over the previous catalysts for degrading aggregated and toxic Aß: (1) High selectivity for aggregated Aß derived from the higher order amyloid structure-recognizing on / off switch for catalyst activity. The precise target selectivity enabled photooxygenation of aggregated A & bgr in the presence of the cells and in mouse brain lysate. (2) low toxicity to the cells. Structural optimization of the catalyst significantly reduced the cytotoxicity both in the dark and under NIR irradiation. (3) high oxygen enrichment under NIR irradiation. Due to the tissue permeability of NIR light, photooxygenation of aggregated A & bgr under the skin of the mouse was possible in high yield. (4) Applicability to the living animal brain in vivo. The injection of the catalyst into the AD model mouse brain, together with the NIR light irradiation, led to a significant decrease in the intact Aβ level in the brain. The results of this study are an important step towards using artificial catalysis as a possible therapeutic strategy against amyloid diseases.


Nobel Prize in Chemistry: Two Americans and a Briton share an award

Nobel Prize in Chemistry goes to a researcher and two researchers

With the results of the investigations in the field of so-called & # 034Directed evolution & # 034, a wide variety of products can be manufactured: from bio-fuels to pharmaceuticals.

The American Frances Arnold shares the award with George Smith and Gregory Winter. Awards for evolution research.

Stockholm / Berlin. With evolution as a model, three protein researchers have created opportunities for more environmentally friendly production of pharmaceuticals and biofuels - and have now received the Nobel Prize in Chemistry for this. Half of the award, endowed with around 870,000 euros (9 million Swedish crowns), goes to the American Frances Arnold (62) and the other half to her compatriot George Smith (77) and the British Gregory Winter (67), like the Royal -Swedish Academy of Sciences announced in Stockholm on Wednesday.

The three researchers have succeeded in controlling evolution and using it for purposes that have brought mankind the greatest benefit. The Nobel Committee calls the American Frances Arnold, the fifth Nobel Prize winner in chemistry to date, the “star of enzyme engineering”, who now works at the California Institute of Technology in Pasadena.

Frances went into research - executive posts would have been too much work

She actually wanted to become a diplomat or CEO of a multinational company. But then the US scientist Frances Arnold decided to research renewable energies because a managerial position would have meant too much work, she said a few months ago.

Their method can be used to optimize molecules such as proteins or DNA. Tailor-made enzymes are used, for example, to produce pharmaceuticals or biofuels - which are often more environmentally friendly than before, as the Nobel Committee emphasizes.

Antibodies against athritis, tumors and Alzheimer's

George Smith developed a method in which so-called bacteriophages - viruses that infect bacteria - are used to create new proteins. Gregory Winter at Cambridge used this process, known as phage display, to develop antibodies for specific purposes. “This achievement was the starting point for a pharmaceutical revolution,” writes the Nobel Committee.

The human antibody adalimumab, which is used against rheumatoid arthritis, among other things, emerged from the work. Antibodies are also used in tumor therapy or researched for the treatment of Alzheimer's disease.

The 67-year-old will head Trinity College in Cambridge until next summer - the facility is considered a forge for Nobel Prize winners. The college has produced more than 30 personalities who have received the high distinction - including in other areas such as literature and peace.

Laser tweezers for holding viruses and cells

On Tuesday, three laser experts were awarded the Nobel Prize in Physics for developing high-precision tools made from light. Half of the award goes to the American Arthur Ashkin (96). The French Gérard Mourou (74) and the Canadian Donna Strickland (59) share the second half.

Millions of patients worldwide benefit from the invention that Mourou and Strickland developed together. The best known is probably the ablation of the cornea by laser, which is carried out millions of times worldwide. The Nobel Committee emphasizes that new drugs, more efficient solar cells or better catalysts could also be produced in the future.

Until the researchers' developments, it was considered science fiction to use the power of light. In the US series “Star Trek”, for example, the spaceship has a tractor beam with which objects can be held and moved. The optical tweezers developed by Ashkin come at least close to this idea: they can be used to hold and move individual bacteria, viruses and living cells with laser beams. Such laser tweezers are now used in a number of laboratories.

Oldest Nobel Prize Winner ever

At 96 years of age, the oldest Nobel Prize winner to date reacted calmly to the award. Ashkin told the Nobel Committee that he could not give interviews, he was very busy with a recent publication.

Strickland reacted more exuberantly to the call from Stockholm: “First you have to think: This is crazy.” Strickland is only the third winner of the Nobel Prize in Physics - 55 years after Maria Goeppert Mayer (1963). Marie Curie had received a Nobel Prize in Physics in 1903. "We have to celebrate women physicists because they are out there," said Strickland. "I am honored to be one of these women."

Immunotherapy against cancer

The winners in medicine were announced on Monday: The American James Allison and the Japanese Tasuku Honjo received the lavish award for the development of immunotherapies against cancer. The ceremonial presentation of the Nobel Prizes traditionally takes place on December 10th, the anniversary of the death of the prize donor Alfred Nobel. (dpa)


Credentials

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[1] Krankenpflege-Fakultät Anhaguera de Ciências e Tecnologia in Brasília



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