Recently, cyclotides have been identified in numerous plant species of the coffee, violet, cucurbit, pea, potato, and grass families. They were originally discovered in Oldenlandia affinis based on their use in traditional African medicine to accelerate labor. These findings provide an alternative view of the mechanism of kB1 bioactivity that corresponds with the concept of an interfacial bioactivity model.Ĭyclotides are plant peptides comprising a circular backbone and three conserved disulfide bonds that confer them with exceptional stability. The interfacial membrane binding of kB1 induced a positive membrane curvature, and the lipids were eventually extracted from the membrane through the kB1 ring-like hollow into the space inside the kB1 cluster.
Our results indicated that the molecules of kB1 were trapped at the membrane-water interface. The conjugation between the wall-like oligomers resulted in the formation of a ring-like hollow in the kB1 cluster on the membrane surface. Two configurations of kB1 oligomers, termed tower-like and wall-like clusters, were detected. The simulations were performed at various concentrations of kB1 to capture the overall progression of its activity. In this study, we conducted coarse-grained molecular dynamics simulations to gain further insight into kB1 bioactivity.
Kalata B1 has been demonstrated to have bioactivity relating to membrane disruption.
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