Abstract
Proteins are currently the fastest-growing class of new therapeutic compounds but smaller proteins and peptides are generally not suitable for use as drugs. Using cyclotides – special knotted proteins stabilized by three pairs of disulphide bonds – as a transport means by grafting onto them as a scaffolding the bioactive peptides can enhance their stability, cellular uptake, and overall efficacy. Experimental methods for creating peptide aptamers are highly time- and resources-consuming. In silico approaches may speed up this process by pre-selecting the drug candidates based on certain biodynamic criteria. In this study, we probe the hypothesis about a relation between the scaffolding conformational stability in conjunction with certain plasticity upon grafting of functionally important domains and the desired biological activity of the modified through the grafting process molecules.
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