Rational design of a reversible pH-responsive switch for peptide self-assembly |
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Authors: | Zimenkov Yuri Dublin Steven N Ni Rong Tu Raymond S Breedveld Victor Apkarian Robert P Conticello Vincent P |
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Institution: | Department of Chemistry and The Integrated Microscopy and Microanalytical Facility, Emory University, 1515 Dickey Drive, Atlanta, GA 30322, USA. |
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Abstract: | Peptide TZ1H, based on the heptad sequence of a coiled-coil trimer, undergoes fully reversible, pH-dependent self-assembly into long-aspect-ratio helical fibers. Substitution of isoleucine residues with histidine at the core d-positions of alternate heptads introduces a mechanism by which self-assembly is coupled to the protonation state of the imidazole side chain. Circular dichroism spectroscopy, transmission electron microscopy, and microrheology techniques revealed that the self-assembly of TZ1H coincides with a distinct coil-helix conformational transition that occurs within a narrow pH range near the pKa of the imidazole side chains of the core histidine residues. |
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