Washington: Scientists have developed synthetic peptides that target and inhibit build up of small, toxic proteins which trigger Alzheimer’s disease. The research, published in the Proceedings of the National Academy of Sciences, may be pave the way for treating the neurodegenerative disorder at an early stage. Alzheimer’s is a disease of aggregation. Neurons in the human brain make a protein called amyloid beta. Such proteins on their own, called monomers of amyloid beta, perform important tasks for neurons. Also Read – Saudi Crown Prince ‘snubbed’ Pak PM, recalled jet from USHowever, in the brains of people with Alzheimer’s disease, amyloid beta monomers have abandoned their jobs and joined together. First, they form oligomers — small clumps of up to a dozen proteins — then longer strands and finally large deposits called plaques. For years, scientists believed that the plaques triggered the cognitive impairments characteristic of Alzheimer’s disease. However, newer research implicates the smaller aggregates of amyloid beta as the toxic elements of this disease. Also Read – Record number of 35 candidates in fray for SL Presidential pollsResearchers at the University of Washington in the US have developed synthetic peptides — which are designed to fold into a structure known as an alpha sheet — can block amyloid beta aggregation at the early and most toxic stage when oligomers form. The team showed that the synthetic alpha sheet’s blocking activity reduced amyloid beta-triggered toxicity in human neural cells grown in culture, and inhibited amyloid beta oligomers in two laboratory animal models for Alzheimer’s. These findings add evidence to the growing consensus that amyloid beta oligomers — not plaques — are the toxic agents behind Alzheimer’s disease. The results also indicate that synthetic alpha sheets could form the basis of therapeutics to clear toxic oligomers in people, according to Valerie Daggett, a professor at University of Washington. “This is about targeting a specific structure of amyloid beta formed by the toxic oligomers,” said Daggett. “What we’ve shown here is that we can design and build synthetic alpha sheets with complementary structures to inhibit aggregation and toxicity of amyloid beta, while leaving the biologically active monomers intact,” she said. The peptides protected laboratory animals from toxic oligomer damage. In brain tissue samples from mice, the team observed an up to 82 per cent drop in amyloid beta oligomer levels after treatment with a synthetic alpha sheet peptide. Administering a synthetic alpha sheet to living mice triggered a 40 per cent drop in amyloid beta oligomer levels after 24 hours. In the common laboratory worm Caenorhabditis elegans, another model for Alzheimer’s disease, treatment with synthetic alpha sheets delayed the onset of amyloid beta-induced paralysis. Daggett’s team is continuing experiments with synthetic alpha sheets to engineer compounds that are even better at clearing amyloid beta oligomers. “What we’re really after are potential therapeutics against amyloid beta and diagnostic measures to detect toxic oligomers in people,” said Daggett.
“Criticism is an important an important aspect of a democracy. I applaud those who criticize me,” the President said adding that he was happy he was able to restore the freedom of expression in the country.The President however said he had informed the SLFP and UPFA leaders including Dinesh Gunawardena and Vasudeva Nanayakkara that he was against granting nominations to former President Mahinda Rajapaksa. He said that all which he was able to achieve with the support of Parliament was possible as he was the President of the SLFP and the UPFA. Sirisena, as President of the Sri Lanka Freedom Party (SLFP) and the United People’s Freedom Alliance (UPFA), has been accused of betraying the January 8 mandate by agreeing to give Rajapaksa nominations from his party. “Mahinda Rajapaksa who was defeated on January 8th will be defeated again,” he said. President Maithripala Sirisena today broke his silence on the issue of granting former President Mahinda Rajapaksa nominations to contest the August 17 Parliament election, and said that he expects Rajapaksa to lose the election.Making a special statement today, Sirisena said that he is very much against Rajapaksa and assured that he will protect the mandate given to him at the January 8 Presidential election. President Sirisena also said that he feels there are many others who are qualified to be the Prime Minister of Sri Lanka.Many expected Sirisena to resign as the SLFP and UPFA President following pressure from the alliance to give Rajapaksa nominations.“If I resigned, anyone Mahinda Rajapaksa wanted would have received nominations,” Sirisena said. On the Central Bank bond controversy, the President said that he had advised Prime Minister Ranil Wickremesinghe to urge the Central Bank Governor to resign.President Sirisena said that he will remain neutral ahead of the August 17 Parliament election and not openly support any political party. (Colombo Gazette)
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