Native load-bearing proteins, such as the muscle protein titin, exhibit a remarkable degree of combined toughness, strength, and elasticity which have yet to be matched by synthetic materials.Single molecule nanomechanical studies on titin and other modular proteins suggest that these exceptional properties arise from a modular elongation mechanism. The sequential unfolding allows modular biopolymers to sustain a large force over the whole extension of the chain, which makes the polymer strong, along with a large area under the force-extension curve, making it tough as well. In addition, when the external force is removed, the unfolded domains of modular proteins will refold automatically, making them elastic. Inspired by nature, one research effort in my group is aimed at designing synthetic macromolecules that form high order structures by programming non-covalent interactions into polymer chain. The goal is to achieve synthetic biomaterials with combined strength, toughness and elasticity. Three classes of well-defined modular polymers have been synthesized in our laboratory: (1) using quadruple hydrogen-bonding motif 2-ureidon-4-pyrimidone (Upy) to direct the formation loops along a polymer chain (J. Am. Chem. Soc. 2004, 126, 2058); (2) using a peptidomimetic beta-sheet based double-closed loop (DCL) as module (J. Am. Chem. Soc. 2004, 126, 14328); and (3) an engineered protein G domain III as module. Single molecule force-extension experiments revealed the sequential unfolding of the loops or domains as these modular polymers are stretched, resulting in sawtooth-patterned curves similar to those seen in titin and other biopolymers. In this paper, we will discuss our designs, syntheses and single-molecule studies of polymers having modular domain structures.