Protein-polyphenol　interactions　are　crucial　in　food　chemistry,　yet　current　detection　methods　have　limitations.　This　study　innovatively　uses　optical　weak　measurement.　Key　variables　like　central　wavelength　shifts　were　measured　in　systems　with　chlorogenic　acid,　tea　polyphenols,　and　various　proteins.　A　linear　relationship　between　polyphenol　concentration　and　wavelength　shift　was　found,　and　a　new　calculation　strategy　for　binding　constants　and　sites　was　developed,　showing　consistent　trends　with　fluorescence　quenching.　The　method　is　label-free　and　applicable　to　non-immobilized　biomolecules,　offering　cost-effective　and　accurate　detection.　However,　it＇s　sensitive　to　solution　fluctuations　and　complex　samples.　Future　research　should　optimize　the　device　and　detection　techniques　to　improve　stability　and　capture　interaction　dynamics.　This　study　provides　a　valuable　tool　for　food　chemistry　research.