The structures of the peptides and their assembly are largely modulated by the environment. To discover the physical principles governing the structural modulations of peptides by the environment would be useful for many applications. As the typical examples, the structures of three kinds of ionic-complementary EAK16-family peptides under various environmental conditions are studied with simulations in this work. A model with intermediate resolution is used, in which both the backbone hydrogen bonds and electrostatic interactions are explicitly considered. The thermodynamics of these peptides (including the free energy and heat capacity) are described for various strengths of the electrostatic interactions which reflect the variation of environment. With these results, the phase diagrams of these peptides related to the temperature and the strength of electrostatic interactions are presented and compared. Based on the differences in the phase structures of the peptide, the different aggregation behaviors are explained based on the monomeric structural features of the peptides. Through the analysis on the stability of various secondary structures of these peptides, it is demonstrated that the charge pattern is the basic reason of the different responses of the EAK16-family peptides to the environmental changes. These results provide some examples and insights for the principles of structural selection by environment and may be helpful for further analysis and designs of peptide systems.