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- W2017156984 abstract "Rigid-rod beta-barrels are composed of interdigitating, short, amphiphilic peptide strands flanked by stabilizing rigid-rod staves. We here report studies on the topological diversity of these recently devised artificial beta-barrels with regard to their length. For this purpose, homologous p-octiphenyl, p-sexiphenyl, and p-quarterphenyl rods were equipped with complementary tripeptide strands based on the sequences Lys-Leu-Lys and Glu-Leu-Glu. The stability of rigid-rod beta-barrels of different length was determined by denaturation with guanidinium chloride. Free energies of delta GH2O = -5.2 kcalmol-1, delta GH2O = -2.9 kcalmol-1, and delta GH2O < -0.3 kcalmol-1 found for homologous p-octiphenyl, p-sexiphenyl, and p-quarterphenyl beta-barrels demonstrated strong dependence of beta-barrel stability on beta-barrel length. These results revealed a very qualitative minimal (approximately 23 A) and an ideal beta-barrel length (approximately 34 A), synergistic formation (alpha = 1.4) and remarkable stability for ideal p-octiphenyl beta-barrels exceeding that of several proteins and most synthetic models. Rigid-rod beta-barrels with p-oligophenyl staves longer than approximately 34 A will be very difficult to make and study because of rapidly decreasing rod solubilities. However, a strategy to bypass this apparent upper limitation of beta-barrel length is introduced: supramolecular matching of mismatched rods yielded elongated beta-barrels (61 A) of acceptable stability (delta GH2O = 2.2 - 3.1 kcalmol-1)." @default.
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- W2017156984 date "2001-01-01" @default.
- W2017156984 modified "2023-10-04" @default.
- W2017156984 title "Topological diversity of artificial ?-barrels in water" @default.
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- W2017156984 doi "https://doi.org/10.1002/1520-636x(2001)13:3<170::aid-chir1016>3.0.co;2-6" @default.
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