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Biotechnologists search for potential drug to treat eye diseases

Associate Professor at the Department of Chemical Engineering, Biotechnology and Environmental Technology, Henrik Karring, has, along with researchers from Aarhus University, found the molecular cause of a range of eye diseases.

The research results, which have just been published in Biochemistry, a respected journal in protein research, show the connection between mutations in the gene encoding protein TGFBIp and the development of opaque corneal deposits in a range of amyloid eye diseases.

"Needle in a haystack" found

The protein TGFBIp is found in high concentration in the cornea. In a range of hereditary diseases, mutations in the TGFBIp gene cause the protein to fold incorrectly, thereby forming amyloid. The accumulation of amyloid results in impaired vision. The TGFBIp protein consists of a total of 638 amino acids and the researchers have now unequivocally found the sequence in the protein which creates amyloid.

"The 18 amino acid long sequence comprises only 2.6% of the whole TGFBIp protein so you could say that we've found a needle in a haystack," says Henrik Karring.

"We have now in two independent research studies and using different methods found the same amyloidogenic sequence of the TGFBIp protein so we are convinced that we have found the right region in the TGFBIp protein," he says.

Collaboration with Griffith University, Australia

On the basis of the new research results, Henrik Karring and PhD student Sanne Ea Jørgensen will now collaborate with Australian researchers in trying to find a drug to treat eye diseases. Sanne E Jørgensen has therefore produced and purified a large amount of normal and mutated TGFBIp which will be used for a large-scale screening of natural chemical products.

"By screening several hundreds to thousands of compounds we hope to find a potential drug against this type of disease," says Sanne Ea Jørgensen.

The research project published in Biochemistry was led by Professor Jan J. Enghild from Aarhus University.

The article from Biochemistry

For more information contact
Associate Professor Henrik Karring, Department of Chemical Engineering, Biotechnology and Environmental Technology, at / cell. +45 2135 6350

Editing was completed: 11.06.2015