Counterion-mediated DNA-condensation is fundamental to most DNA related activity in cells, from chromosome packaging to control over translational mechanisms. Developed synthetic systems for manipulation of DNA-condensation could prove essential for development of biotechnologies for gene encapsulation and DNA-separation. Dynamics of DNA-condensation are studied using a model peptide where interaction between DNA and peptide is non-specific. This model uses a designed peptide showing switchable surface activity, where the folded form of the peptide is amphiphilic and the unfolded form is not. The peptide is α-helical, containing 23 amino acids with variation in the number and distribution of hydrophobic and charged amino acids. This design incorporates hydrophobic residues on one side (leucines and alanines) and hydrophilic residues on the opposite so that helix is surface active. The secondary structure is characterized by using circular dichroism spectropolarimetry, showing that the peptide has a transient secondary structure as a function of monovalent salt concentration. This peptide behavior at the air-water interface can be characterized by pendant drop/bubble methods and modeled accordingly. Our hypothesis is that the unfolded peptide is in equilibrium with the folded peptide in the bulk solution, but, in presence of DNA, the unfolded peptide folds and then binds to it. The critical aggregate concentration of the peptide for DNA condensation is determined using multi-angle light scattering, which is also used to calculate the radius of gyration and molecular weight of these condensates. The kinetics of the condensation process are studied using circular dichroism in Stop-flow mode and also by isothermal titration calorimetry.