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Study shows short peptides can self-assemble into catalysts

Posted March 17, 2014
Study shows short peptides can self-assemble into catalysts
Overview of concept and design. a, Structure of human carbonic anhydrase showing a typical metal-binding motif. b, Model for one of the designed peptides (11, Ac-IHIHIQI-CONH2) in the extended b-strand configuration showing positions of the residues in the sequence. c–e, Computationally derived model of fibrils formed by 11, showing overall fold (c), packing of the hydrophobic core (d) and zinc primary coordination sphere (e). Credit:Nature Chemistry (2014) doi:10.1038/nchem.1894
A team of researchers with members from Syracuse University and the University of California, has found that naturally forming peptides can self-assemble into catalysts. In their paper published in the journal Nature Chemistry, the team describes how they designed seven peptides, allowed the resulting molecules to self-assemble into amyloids and then noted how many of them could catalyze the hydrolysis of esters.

Scientists have long wondered how enzymes could have possibly come to exist in the primordial soup that existed on Earth so long ago, leading to life as we know it. Enzymes, necessary for metabolic reactions, are made of large complicated (folded into three dimensions) proteins, with long chains of amino acids. That they could self-assemble into the structures we see today seems nearly impossible, even given millions of years (leading to the belief by some of the idea of intelligent design).

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