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- Title
In silico approach to probe the binding affinity between OMVs harboring the Z<sub>EGFR</sub> affibody and the EGF receptor.
- Authors
Sepahdar, Zahra; Saghiri, Reza; Miroliaei, Mehran; Salimi, Mona
- Abstract
There is a growing interest in designing a nanocarrier containing an EGFR targeting affibody to direct toward cancer cells. Here, cytolysin A was cloned at the N-terminus of ZEGFR:1907 affibody to guarantee its surface presentation on the OMVs while targeting the epidermal growth factor receptors (EGFRs). A separate construct including a fusogenic peptide (GALA) was also designed for the endosomal escape of the nanocarrier. Binding of the two constructs ClyA-affiEGFR and ClyA-affiEGFR-GALA to domain III of EGFR was investigated using molecular docking and molecular dynamic simulations. The higher stability of the ClyA-affiEGFR-GALA/EGFR as compared to the ClyA-affiEGFR/EGFR complex was evident. The ClyA-affiEGFR-GALA structure showed a higher RMSD during the first half of the simulation time implying a much less stable behavior. Plateau state of the radius of gyration plot of ClyA-affiEGFR-GALA confirmed a well-folded structure in the presence of the GALA sequence. Solvent accessible surface area for both proteins was in the same range. The data obtained from hydrogen bond analysis revealed a more equilibrated and stable form of the ClyA-affiEGFR-GALA structure upon interaction with EGFR. The data provided here was a requisite for our biological evaluation of the synthesized constructs as a component of a novel drug delivery system.
- Subjects
EPIDERMAL growth factor receptors; PEPTIDES; DRUG delivery systems
- Publication
Journal of Molecular Modeling, 2022, Vol 28, Issue 5, p1
- ISSN
1610-2940
- Publication type
Article
- DOI
10.1007/s00894-022-05043-9