Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation

作者：Ito Len^*; Shiraki Kentaro; Makino Masatomo; Hasegawa Kazuya; Kumasaka Takashi

来源：FEBS Letters, 2011, 585(3): 555-560.

DOI：10.1016/j.febslet.2011.01.008

• Glycine amide
• Crystal structure
• Lysozyme
• Protein aggregation
• Accessible surface area

Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated. Here, we show the crystal structure of the GlyAd-lysozyme complex by high resolution X-ray crystallographic analysis at a 1.05 angstrom resolution. GlyAd bound to the lysozyme surface near aromatic residues and decreased the amount of bound waters and increased the mobility of protein. Arg and GlyAd molecules are different in binding sites and patterns from glycerol and related compounds, indicating that decreasing hydrophobic patches might be involved in suppression of protein aggregation.

• 出版日期2011-2-4