A zwitterionic polymer as a novel inhibitor of protein aggregation

H-NMR before and after aggregation revealed the conformational changes taking place in the lysozyme: during aggregation, lysozyme is transformed into a random coil conformation, thus losing its secondary structure. Presence of the polymer facilitates retention of partial higher order structures and lysozyme solubility at higher temperatures. The high efficiency of the polyampholyte was ascribed to its ability to prevent collisions between aggregating species by acting as a molecular shield.