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Prog Mol Biol Transl Sci. 2013;117:53-72. doi: 10.1016/B978-0-12-386931-9.00003-9.

Physicochemical principles of protein aggregation.

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Centre for Genomic Regulation, CRG and UPF, Barcelona, Spain.


This chapter provides a theoretical framework on the quantitative description of protein aggregation. The reader is provided with an overview of the fundamental theory of linear and helical polymers, as well as an introduction on the parameters governing evolution of aggregates over time. The models presented for the interpretation of the protein aggregation process take into account the contributions of different physicochemical parameters such as charge, hydrophobicity, and secondary structure propensity. Finally, we discuss our current understanding of how prediction of aggregation rates and identification of aggregation-prone protein regions are predicted from the information contained in the primary amino acid sequence.

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