Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme

Wen Sing Wen, Jun Kun Lai, Yu Jiun Lin, Chia Min Lai, Yun Chiao Huang, Steven S.S. Wang, Jeng-Shiung Jan

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)107-116
Number of pages10
JournalBiopolymers
Volume97
Issue number2
DOIs
Publication statusPublished - 2012 Jan 1

Fingerprint

Egg White
Polypeptides
Muramidase
Amyloid
Enzymes
Glycine
Peptides
Lysine
Amino acids
Amyloidogenic Proteins
Hydrogen Bonding
Chemical analysis
Phenylalanine
Hydrophobic and Hydrophilic Interactions
Hydrogen bonds
Polymers
Monomers
Association reactions
Proteins
hen egg lysozyme

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Wen, W. S., Lai, J. K., Lin, Y. J., Lai, C. M., Huang, Y. C., Wang, S. S. S., & Jan, J-S. (2012). Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme. Biopolymers, 97(2), 107-116. https://doi.org/10.1002/bip.21707
Wen, Wen Sing ; Lai, Jun Kun ; Lin, Yu Jiun ; Lai, Chia Min ; Huang, Yun Chiao ; Wang, Steven S.S. ; Jan, Jeng-Shiung. / Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme. In: Biopolymers. 2012 ; Vol. 97, No. 2. pp. 107-116.
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Wen, WS, Lai, JK, Lin, YJ, Lai, CM, Huang, YC, Wang, SSS & Jan, J-S 2012, 'Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme', Biopolymers, vol. 97, no. 2, pp. 107-116. https://doi.org/10.1002/bip.21707

Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme. / Wen, Wen Sing; Lai, Jun Kun; Lin, Yu Jiun; Lai, Chia Min; Huang, Yun Chiao; Wang, Steven S.S.; Jan, Jeng-Shiung.

In: Biopolymers, Vol. 97, No. 2, 01.01.2012, p. 107-116.

Research output: Contribution to journalArticle

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Wen WS, Lai JK, Lin YJ, Lai CM, Huang YC, Wang SSS et al. Effects of copolypeptides on amyloid fibrillation of hen egg-white lysozyme. Biopolymers. 2012 Jan 1;97(2):107-116. https://doi.org/10.1002/bip.21707