| (a) aggregation resistance by modifying antigen binding sites |
scFv stability improved
by creating aggregation-resistant mutants |
modifying
antigen binding sites is cumbersome and could potentially
impact antigen binding ability |
| (b) modifying net antibody charge |
CDRs
left unmodified; as such the impact on antigen binding
ability is less likely to be affected |
requires mutation
of sites along an antibody—which is a still a cumbersome method |
| (c) cell envelope compositions |
simple
strategy to stabilize biomolecules (i.e., scFv), with
limited to no further processing steps required—antibody fragment
is left in its native cell envelope environment; can be kept intact
or fragmented depending on application; could be lyophilized for long-term storage; cell surfaces allow for multiple
scFvs, which provide a multivalent avidity effect for protein capture |
not suited to some applications where the native cell wall
could interfere with the surrounding environment; potential for cell
fragments to aggregate; possibility of nonspecific absorption if fragment
size is not optimized; considerations of biomolecule (i.e., scFv)
cell-surface heterogeneity expression needs to be undertaken |
