Protein aggregation is not only a common problem in biopharmaceutical industry involving protein drugs,but also a devastating phenomenon closely linked to numerous human diseases.Understanding structural details of protein aggregates is fundamentally important in the prediction and prevention of protein aggregation behavior.In this study,we explore to use a turbidity-based dissociation kinetic assay to tackle the complex nature of protein amorphous aggregates by a model protein,bovine serum albumin(BSA).We observe that the dissociation of BSA aggregates under basic condition consists of four distinct kinetic phases,including a burst phase,two relatively slow phases,and one kinetically inert phase.Such kinetic observation allows us to hypothesize that BSA aggregates consist of at least four different types of BSA monomeric structures at the molecular level.To the best of our knowledge,this is the first turbidity-based investigation with the aim to elucidate the structural heterogeneity of protein amorphous aggregates.
LI Haoyi
,
LI Dongmin
,
MA Gang
,
SHANG Yanli
,
SUN Ying
. Structural insights into bovine serum albumin aggregates by a dissociation kinetic investigation[J]. Journal of Hebei University(Natural Science Edition), 2016
, 36(1)
: 35
-42
.
DOI: 10.3969/j.issn.1000-1565.2016.01.007
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