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000858403 1001_ $$00000-0003-4628-526X$$aOrr, Asuka A.$$b0
000858403 245__ $$aElucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins
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000858403 520__ $$aβ-wrapins are engineered binding proteins stabilizing the β-hairpin conformations of amyloidogenic proteins islet amyloid polypeptide (IAPP), amyloid-β, and α-synuclein, thus inhibiting their amyloid propensity. Here, we use computational and experimental methods to investigate the molecular recognition of IAPP by β-wrapins. We show that the multi-targeted, IAPP, amyloid-β, and α-synuclein, binding properties of β-wrapins originate mainly from optimized interactions between β-wrapin residues and sets of residues in the three amyloidogenic proteins with similar physicochemical properties. Our results suggest that IAPP is a comparatively promiscuous β-wrapin target, probably due to the low number of charged residues in the IAPP β-hairpin motif. The sub-micromolar affinity of β-wrapin HI18, specifically selected against IAPP, is achieved in part by salt-bridge formation between HI18 residue Glu10 and the IAPP N-terminal residue Lys1, both located in the flexible N-termini of the interacting proteins. Our findings provide insights towards developing novel protein-based single- or multi-targeted therapeutics.
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000858403 7001_ $$0P:(DE-Juel1)167315$$aShaykhalishahi, Hamed$$b1
000858403 7001_ $$0P:(DE-HGF)0$$aMirecka, Ewa A.$$b2
000858403 7001_ $$00000-0001-7327-238X$$aJonnalagadda, Sai Vamshi R.$$b3
000858403 7001_ $$0P:(DE-Juel1)166306$$aHoyer, Wolfgang$$b4$$eCorresponding author
000858403 7001_ $$00000-0002-3342-2651$$aTamamis, Phanourios$$b5$$eCorresponding author
000858403 773__ $$0PERI:(DE-600)1499971-7$$a10.1016/j.compchemeng.2018.02.013$$gVol. 116, p. 322 - 332$$p322 - 332$$tComputers & chemical engineering$$v116$$x0098-1354$$y2018
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