The　non-covalent　interaction　of　tryptophan(L-Trp)　with　adipic　dihydrazide(ADH),　diacetone　acrylamide(DAAM)　or　acrylic　acid(AA)　was　investigated　by　fluorescence　quenching,　three-dimensional　fluorescence　spectrum　in　combination　with　computer　simulation,　respectively.　The　quenching　mechanism,　the　strength　and　types　of　interaction　force　between　L-Trp　and　functional　monomers　were　studied.　The　results　showed　that　the　fluorescence　of　L-Trp　was　quenched　through　a　static　quenching　procedure　by　functional　monomer　due　to　the　formation　of　L-Trp-functional　monomer　complexes.　The　complexes　had　high　binding　constant　and　exhibited　good　stability.　The　non-covalent　interaction　between　L-Trp　and　functional　monomers　was　dominated　by　hydrogen　bond　and　electrostatic　force.　The　binding　site　in　L-Trp　was　supplied　largely　by　carboxyl　group　rather　than　heteroaromatic　ring.　The　strength　of　interaction　between　L-Trp　and　functional　monomers　was　in　the　following　order:　L-Trp-ADH＞L-Trp-DAAM＞L-Trp-AA.