Understanding the basic forces that determine molecular recognition helps t
o elucidate mechanisms of biological processes and facilitates discovery of
innovative biotechnological methods and materials for therapeutics, diagno
stics, and separation science. The ability to measure interaction propertie
s of biological macromolecules quantitatively across a wide range of affini
ty, size, and purity is a growing need of studies aimed at characterizing b
iomolecular interactions and the structural elements that drive them. Optic
al biosensors have provided an increasingly impactful technology for such b
iomolecular interaction analyses. These biosensors record the binding and d
issociation of macromolecules in real time by transducing the accumulation
of mass of an analyte molecule at the sensor surface coated with ligand mol
ecule into an optical signal. Interactions of analytes and ligands can be a
nalyzed at a microscale and without the need to label either interactant. S
ensors enable the detection of bimolecular interaction as well as multimole
cular assembly. Most notably, the method is quantitative and kinetic, enabl
ing determination of both steady-state and dynamic parameters of interactio
n. This article describes the basic methodology of optical biosensors and p
resents several examples of its use to investigate such biomolecular system
s as cytokine growth factor-receptor recognition, coagulation factor assemb
ly, and virus-cell docking (C) 1999 Academic Press.