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

Abstract:

: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 1.05Å 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ito L,Shiraki K,Makino M,Hasegawa K,Kumasaka T

doi

10.1016/j.febslet.2011.01.008

subject

Has Abstract

pub_date

2011-02-04 00:00:00

pages

555-60

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(11)00029-9

journal_volume

585

pub_type

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