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The reassembly of a half-sequence ionic self-complementarity peptide CH3CO-Pro-Ser-Phe-Cys-Phe-Lys-Phe-Glu-Pro-NH2 was reported, which could self-assemble into stable nanofibers and formed hydrogel consisting of >99% water. In this study, the nanofiber scaffold was sonicated by an ultrasonic cell disruptor. The effects of sonication were detected by circular dichroism (CD), atomic force microscopy (AFM), and rheology. AFM image illustrated that the sonicated fragments could quickly reassemble into nanofibers, while the morphology was distinguishable from the original one. CD spectrum revealed that the conversion occurred mainly between regular β-strand structure and distorted β-strand structure. Rheological analyses showed that the storage modulus (G’) of the peptide solution at the 7th day after sonication decreased by nearly 40% compared with the value of the solution before sonication. Finally, a plausible conversion model was proposed to interpret the reassembly process.
The reassembly of a half-sequence ionic self-complementarity peptide CH3CO-Pro-Ser-Phe-Cys-Phe-Lys-Phe-Glu-Pro-NH2 was reported, which could be self- assembled into stable nanofibers and formed hydrogel consisting of> 99% water. In this study, the nanofiber sc s sold was sonicated by an ultrasonic cell disruptor. The effects of sonication were detected by circular dichroism (CD), atomic force microscopy (AFM), and rheology. AFM image illustrated that the sonicated fragments could quickly reassemble into nanofibers, while the morphology was distinguishable from the original one. CD spectrum revealed that the conversion occurred primarily between regular β-strand structure and distorted β-strand structure. Rheological analyzes showed that the storage modulus (G ’) of the peptide solution at the 7th day after sonication decreased by nearly 40% compared with the value of the solution before sonication. Finally, a plausible conversion model was proposed to interpret the reassembly process.