Protein
adsorption onto polymer surfaces is a very complex, ubiquitous, and
integrated process, impacting essential areas of food processing and
packaging, health devices, diagnostic tools, and medical products.
The nature of protein–surface interactions is becoming much
more complicated with continuous efforts toward miniaturization, especially
for the development of highly compact protein detection and diagnostic
devices. A large body of literature reports on protein adsorption
from the perspective of ensemble-averaged behavior on macroscopic,
chemically homogeneous, polymeric surfaces. However, protein–surface
interactions governing the nanoscale size regime may not be effectively
inferred from their macroscopic and microscopic characteristics. Recently,
research efforts have been made to produce periodically arranged,
nanoscopic protein patterns on diblock copolymer surfaces solely through
self-assembly. Intriguing protein adsorption phenomena are directly
probed on the individual biomolecule level for a fundamental understanding
of protein adsorption on nanoscale surfaces exhibiting varying degrees
of chemical heterogeneity. Insight gained from protein assembly on
diblock copolymers can be effectively used to control the surface
density, conformation, orientation, and biofunctionality of prebound
proteins in highly miniaturized applications, now approaching the
nanoscale. This feature article will highlight recent experimental
and theoretical advances made on these fronts while focusing on single-biomolecule-level
investigations of protein adsorption behavior combined with surface
chemical heterogeneity on the length scale commensurate with a single
protein. This article will also address advantages and challenges
of the self-assembly-driven patterning technology used to produce
protein nanoarrays and its implications for ultrahigh density, functional,
and quantifiable protein detection in a highly miniaturized format.