In Silico Structural Modeling and Analysis of Physicochemical Properties of Antitumoral QS‐13 Peptide and Its Derivatives in Water and Dimethyl Sulfoxide
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Media type:
E-Article
Title:
In Silico Structural Modeling and Analysis of Physicochemical Properties of Antitumoral QS‐13 Peptide and Its Derivatives in Water and Dimethyl Sulfoxide
Description:
ABSTRACTThe NC1 domain of the alpha 4 chain of type IV collagen was previously reported to exert anti‐tumor properties in a melanoma model and to inhibit angiogenesis. The minimal active sequence identified to date comprises 13 amino acids: QKISRCQVCVKYS. Unfortunately, this sequence is not soluble in aqueous media and requires prior dissolution in DMSO. The disulfide bridge (DB) that spontaneously forms in solution between two cysteine residues is crucial for its biological activity. The aim of this article was to study the impact of DMSO on the physicochemical properties of the QS‐13 peptide and to replace hydrophobic amino acids to enhance its water solubility. Using bioinformatics (GROMACS, VMD, and ProtParam) and programming (Python and RStudio) software programs, we demonstrated that DMSO could promote the formation of DBs, but it is not strictly necessary. Among the QS‐13 substituted peptides, some were demonstrated to display similar characteristics to the original peptide. Improved water solubility will make the peptide easier to use in biological studies and facilitate its administration for potential therapeutic applications.