Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2

A. A. Moosavi-Movahedi; P. Pirzadeh; S. Hashemnia; S. Ahmadian; B. Hemmateenejad; M. Amani; A. A. Saboury; F. Ahmad; M. Shamsipur; G. H. Hakimelahi; Fu Yuan Tsai; H. Hadi Alijanvand; R. Yousefi

doi:10.1016/j.colsurfb.2007.05.018

Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2

A. A. Moosavi-Movahedi^*, P. Pirzadeh, S. Hashemnia, S. Ahmadian, B. Hemmateenejad, M. Amani, A. A. Saboury, F. Ahmad, M. Shamsipur, G. H. Hakimelahi, Fu Yuan Tsai, H. Hadi Alijanvand, R. Yousefi

^*Corresponding author for this work

Center for General Education

Research output: Contribution to journal › Journal Article › peer-review

35 Scopus citations

Abstract

Fibril formation seems to be a general property of all proteins. Its occurrence in hen or human lysozyme depends on certain conditions, namely acidic pHs or the presence of some additives. This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Based on observations such as the strange increase in absorbance at 650 nm (pH 9.2) and the presence of intermediates, it is assumed that lysozyme fibrils have been formed at pH 9.2 in the presence of SDS as an anionic surfactant. Thioflavin T emission fluorescence and an EM image confirmed this assumption. β-cyclodextrin was then used as a turbidity inhibitor to establish its effect on the distribution of intermediates that participate in fibril formation.

Original language	English
Pages (from-to)	55-61
Number of pages	7
Journal	Colloids and Surfaces B: Biointerfaces
Volume	60
Issue number	1
DOIs	https://doi.org/10.1016/j.colsurfb.2007.05.018
State	Published - 15 10 2007

Keywords

Chemometry
Electron microscopy
Fibril
Lysozyme
Sodium dodecyl sulfate
β-Cyclodextrin

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10.1016/j.colsurfb.2007.05.018

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Moosavi-Movahedi, A. A., Pirzadeh, P., Hashemnia, S., Ahmadian, S., Hemmateenejad, B., Amani, M., Saboury, A. A., Ahmad, F., Shamsipur, M., Hakimelahi, G. H., Tsai, F. Y., Alijanvand, H. H., & Yousefi, R. (2007). Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2. Colloids and Surfaces B: Biointerfaces, 60(1), 55-61. https://doi.org/10.1016/j.colsurfb.2007.05.018

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title = "Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2",

abstract = "Fibril formation seems to be a general property of all proteins. Its occurrence in hen or human lysozyme depends on certain conditions, namely acidic pHs or the presence of some additives. This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Based on observations such as the strange increase in absorbance at 650 nm (pH 9.2) and the presence of intermediates, it is assumed that lysozyme fibrils have been formed at pH 9.2 in the presence of SDS as an anionic surfactant. Thioflavin T emission fluorescence and an EM image confirmed this assumption. β-cyclodextrin was then used as a turbidity inhibitor to establish its effect on the distribution of intermediates that participate in fibril formation.",

keywords = "Chemometry, Electron microscopy, Fibril, Lysozyme, Sodium dodecyl sulfate, β-Cyclodextrin",

author = "Moosavi-Movahedi, {A. A.} and P. Pirzadeh and S. Hashemnia and S. Ahmadian and B. Hemmateenejad and M. Amani and Saboury, {A. A.} and F. Ahmad and M. Shamsipur and Hakimelahi, {G. H.} and Tsai, {Fu Yuan} and Alijanvand, {H. Hadi} and R. Yousefi",

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doi = "10.1016/j.colsurfb.2007.05.018",

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Moosavi-Movahedi, AA, Pirzadeh, P, Hashemnia, S, Ahmadian, S, Hemmateenejad, B, Amani, M, Saboury, AA, Ahmad, F, Shamsipur, M, Hakimelahi, GH, Tsai, FY, Alijanvand, HH & Yousefi, R 2007, 'Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2', Colloids and Surfaces B: Biointerfaces, vol. 60, no. 1, pp. 55-61. https://doi.org/10.1016/j.colsurfb.2007.05.018

TY - JOUR

T1 - Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2

AU - Moosavi-Movahedi, A. A.

AU - Pirzadeh, P.

AU - Hashemnia, S.

AU - Ahmadian, S.

AU - Hemmateenejad, B.

AU - Amani, M.

AU - Saboury, A. A.

AU - Ahmad, F.

AU - Shamsipur, M.

AU - Hakimelahi, G. H.

AU - Tsai, Fu Yuan

AU - Alijanvand, H. Hadi

AU - Yousefi, R.

PY - 2007/10/15

Y1 - 2007/10/15

N2 - Fibril formation seems to be a general property of all proteins. Its occurrence in hen or human lysozyme depends on certain conditions, namely acidic pHs or the presence of some additives. This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Based on observations such as the strange increase in absorbance at 650 nm (pH 9.2) and the presence of intermediates, it is assumed that lysozyme fibrils have been formed at pH 9.2 in the presence of SDS as an anionic surfactant. Thioflavin T emission fluorescence and an EM image confirmed this assumption. β-cyclodextrin was then used as a turbidity inhibitor to establish its effect on the distribution of intermediates that participate in fibril formation.

AB - Fibril formation seems to be a general property of all proteins. Its occurrence in hen or human lysozyme depends on certain conditions, namely acidic pHs or the presence of some additives. This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Based on observations such as the strange increase in absorbance at 650 nm (pH 9.2) and the presence of intermediates, it is assumed that lysozyme fibrils have been formed at pH 9.2 in the presence of SDS as an anionic surfactant. Thioflavin T emission fluorescence and an EM image confirmed this assumption. β-cyclodextrin was then used as a turbidity inhibitor to establish its effect on the distribution of intermediates that participate in fibril formation.

KW - Chemometry

KW - Electron microscopy

KW - Fibril

KW - Lysozyme

KW - Sodium dodecyl sulfate

KW - β-Cyclodextrin

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U2 - 10.1016/j.colsurfb.2007.05.018

DO - 10.1016/j.colsurfb.2007.05.018

M3 - 文章

C2 - 17616361

AN - SCOPUS:34548164833

SN - 0927-7765

VL - 60

SP - 55

EP - 61

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

IS - 1

ER -

Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2

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Keywords

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