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Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme†
Article first published online: 19 AUG 2011
Copyright © 2011 Wiley Periodicals, Inc.
Volume 97, Issue 2, pages 107–116, February 2012
How to Cite
Wen, W.-S., Lai, J.-K., Lin, Y.-J., Lai, C.-M., Huang, Y.-C., Wang, S. S.-S. and Jan, J.-S. (2012), Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme. Biopolymers, 97: 107–116. doi: 10.1002/bip.21707
- Issue published online: 23 NOV 2011
- Article first published online: 19 AUG 2011
- Manuscript Accepted: 25 JUL 2011
- Manuscript Revised: 19 JUL 2011
- Manuscript Received: 8 DEC 2010
- National Science Council. Grant Numbers: NSC99-2628-E-006-003, NSC98-2221-E-002-063-MY3
- amyloid fibril;
- attenuation of fibrillation;
The fibrillation of hen egg-white lysozyme (HEWL) in the absence and presence of simple, unstructured D,L-lysine-co-glycine (D,L-Lys-co-gly) and D,L-lysine-co-L-phenylalanine (D,L-Lys-co-Phe) copolypeptides was studied by using a variety of analytical techniques. The attenuating and decelerating effects on fibrillation are significantly dependent on the polypeptide concentration and the composition ratios in the polypeptide chain. Interestingly, D,L-Lys-co-gly and D,L-Lys-co-Phe copolypeptides with the same composition ratio have comparable attenuating effects on fibrillation. The copolypeptide with highest molar fraction of glycine residue exhibits the strongest suppression of HEWL fibrillation. The copolypeptide has the highest hydrophobic interacting capacity due to the more molar ratio of apolar monomer in the polymer backbone. The major driving forces for the association of HEWL and copolypeptides are likely to be hydrogen bonding and hydrophobic interactions, and these interactions reduce the concentration of free protein in solution available to proceed to fibrillation, leading to the increase of lag time and attenuation of fibrillation. The results of this work may contribute to the understanding of the molecular factors affecting amyloid fibrillation and the molecular mechanism(s) of the interactions between the unstructured polypeptides and the amyloid proteins. © 2011 Wiley Periodicals, Inc. Biopolymers 97:107–116, 2012.