WSEAS Transactions on Biology and Biomedicine
Print ISSN: 1109-9518, E-ISSN: 2224-2902
Volume 23, 2026
Computer Simulation of Complexation of GluAsp Peptide Molecules and Lysine-Based Dendrimer with ArgHis Spacers
Authors: , , , , ,
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Abstract: Lysine-based dendrimers of the second generation containing alanine, glycine, lysine, arginine, and leucine spacers (2Ala, 2Gly, 2Lys, 2Arg, and 2Leu), as well as double histidine (2His) spacers inserted between their branching points, have been studied earlier. This study examined the complexes formed by bioactive GluAsp peptide and dendrimer that contain an arginine-histidine (ArgHis) spacer. The main difference from previous studies is that amino acid residues (Arg and His) in the dendrimer spacers are not the same. We con-ducted molecular simulations to study the interactions of 16 GluAsp molecules and a single dendrimer with neutral histidines (His) and with fully charged histidines (Hisp) in an aqueous solution containing explicit coun-terions. We have shown that the complex of the dendrimer with protonated Hisp residues in spacers contains a larger number of GluAsp molecules, which penetrate deeper into the center of this dendrimer than in the same dendrimer with neutral His.
Keywords:
Stimuli-responsive molecules, histidine-containing lysine dendrimers, oligopeptides, complexes, computer simulation, molecular dynamics
Pages: 218-224
DOI: 10.37394/23208.2026.23.20