The　mechanisms　of　interaction　between　bovine　serum　albumin　(BSA)　with　Rhodamine　B　(RB)　have　been　investigated　using　fluorescence　spectroscopy.　The　quenching　of　fluorescence　from　BSA　takes　place　when　increasing　the　RB　concentration.　Similar　fluorescence　quenching　from　RB　also　takes　place　when　increasing　the　BSA　concentration.　Dual　quenching　is　attributed　to　the　binding　of　RB　to　BSA　and　the　energy　transfer　between　BSA　and　RB.　In　this　interaction,　BSA　as　well　as　RB　acts　as　both　donor　and　acceptor.　Furthermore,　increasing　the　concentration　of　RB　also　leads　to　BSA　fluorescence　peak　splitting　at　345　nm.　Therefore,　not　only　the　intensity,　but　also　shape　and　peak　position　of　the　fluorescence　spectrum　from　BSA　are　controllable　by　the　concentration　of　RB.　This　multi-information　fluorescence　probe　method　indicates　potential　applications　in　bio-optical　sensor.　(C)　2009　Elsevier　B.V.　All　rights　reserved.