The results are presented to firstly show the effect of charge on intermolecular repulsion under physiological selfassembly of glutamine-containing peptides, then the effect of molecular attraction is explored through the degree of hydrogen bonding by comparing three different serine-containing peptides to three glutamine-containing equivalent peptides. Finally, based on these findings, we demonstrate formation of a hybrid hydrogel formed from a mixture of non-gelling P11 peptides. To aid the reader in correlating the peptide number (N) in the P11 series with its charge and peripheral amino acid type and net charge, we use the nomenclature P11-N (a,b), where a are the peripheral amino acids (Q for glutamine; S for serine) and b is the net charge of the peptide at physiological pH.