The gelation kinetics of four beta-hairpin oligopeptides that have been designed to exhibit responsive behavior to changes in environmental conditions, such its pH, ionic strength and temperature, are characterized using multiple particle tracking microrheology and circular dichroism (CD) spectroscopy. The peptides, predominantly all alternating sequence of valine and lysine residues, differ by a point substitution Of It single amino acid near a type II' beta-turn sequence. The rate of gelation becomes faster for point substitutions which reduce the total charge of the peptide. Similarly, increasing the ionic strength reduces or screens intra- and intermolecular electrostatic repulsions, again leading to faster gelation kinetics. CD measurements show that the concentration of Folded peptide at the gel point decreases as the gelation kinetics become slower, possibly indicating it relationship between the assembly rate and the resulting gel microstructure Finally. a model is developed based oil the electrostatic barrier to peptide folding and association which agrees semiquantitatively with the microrheology results. This represents it first step toward understanding the role of peptide charge and physicochemical conditions in the self-assembly of these peptide hydrogelators