Inhibition of tyrosinase and elastase is required to control skin pigmentation and inflammation. Only a few plant phenols provide a balanced inhibition of both enzymes (Koganov & Duev, MARM 2007). Optimization of topical products requires further investigation of interactions among selected phenols and components of delivery system because certain polymers capable of modulating the activity of enzymes associated with skin inflammation (Koganov, US 20050175579). Twenty phenols with common structure: C₁₅ (C₆�C₃�C₆) flavone nucleus including two benzene rings (A & B) linked through O-containing pyran or pyrone ring (C) were investigated. Conjugated π bonds in A and B rings and π bond between C2 and C3 play an important role in tyrosinase and elastase inhibition. Presence of 6-O-α-L-rhamnosyl-D-glucose at C3 decreased the activity of phenol. Presence of 4-hydroxyphenyl or 3,4,5-trihydroxy-benzoil at C3 and of 3,4-dihydroxyphenyl at C2 significantly increased enzyme inhibitory activities. Hydroxylation in positions B3', B5', C3 also increased inhibitory activities. Selected acrylic polymers potentiate elastase inhibition of certain phenols. However, these polymers were inactive against tyrosinase and didn't affect tyrosinase inhibition activity of phenols. Enzymes inhibition in systems containing most active polymers and phenols (Rosmarinic Acid � RMA and Epigallocatechin Gallate � EGCG) were analyzed. RMA's elastase inhibitory activity includes electrostatic interactions. Tyrosinase inhibition by RMA is relatively insensitive to electrolyte concentration. EGCG's inhibitory effect of both enzymes includes hydrophobic interactions. When applied together, RMA competes with EGCG for tyrosinase and elastase inhibition. Development of novel skin whitening/lightening and anti-inflammatory ingredients and optimization of delivery systems will be discussed.