Benzene-1,3,5-tricarboxamide (BTA) is an ideal monomeric subunit for a synthetic extracellular matrix (ECM) as it self assembles in water to form fibers similar to collagen. In order to replicate the ECM’s ability to enhance the bioavailability of enzymes and molecules, an arm extending from the BTA hydrophobic center was functionalized in 69 percent yield for attachment of the S- peptide in an azide-alkyne cycloaddition reaction yielding 49 percent. The BTA-peptide  conjugate incorporates at fifty percent molar volume in self-assembling BTA fibers, verified by characteristic absorption peaks at 310 and 330 nm using UV-Vis spectrophotometry. In comparison, the azide-functionalized, monoextended BTA subunit incorporates at 10 percent molar volume into BTA fibers.