 Introducing rational mutations into anti-ABeta antibodies to increase their effectiveness and remove harmful side reactions is a way forward, but the path to take is unclear since the key structural characteristics that determine the binding affinity and selectivity of anti-ABeta antibodies towards amyloid species are not well understood .
<coherence>  Introducing rational mutations into anti-ABeta antibodies to increase their effectiveness and remove harmful side reactions is a way forward, but the path to take is unclear since the key structural characteristics that determine the binding affinity and selectivity of anti-ABeta antibodies towards amyloid species are not well understood .
 Introducing rational mutations into anti-ABeta antibodies to increase their effectiveness is a way forward, but the path to take is unclear since the key structural characteristics that determine the binding affinity and selectivity of anti-ABeta antibodies towards amyloid species are not well understood .