Biphasic Role of β-Cyclodextrin in Anionic Surfactant-induced Lysozyme Aggregation and Refolding
Abstract
This study explores the role of β-cyclodextrin (β-CD) on the aggregation and refolding of hen egg white lysozyme (HEWL) induced by an anionic surfactant, i.e., sodium dodecylbenzenesulfonate (SDBS). Different biophysical techniques (Spectrophotometer, Flurometer, and Circular Dichroism) were employed to measure the conformational changes and aggregation propensity. UV-Vis spectroscopy revealed a biphasic turbidity response: initial β-CD concentrations (<0.4 mM) enhanced HEWL aggregation, whereas higher concentrations (>0.4 mM) solubilized the SDBS-induced aggregates, thereby restoring a native-like HEWL structure. Intrinsic fluorescence and circular dichroism analyses indicated that β-CD mitigated SDBS-induced structural disruptions, facilitating HEWL refolding. Thioflavin T assays confirmed the formation of amyloid-like fibrils in the SDBS-HEWL complex, which were solubilized upon addition of higher β-CD concentration, correlating with a decrease in turbidity,the regain of tertiary and secondary structure. Right-angle light scattering kinetic measurements supported these findings, showing rapid aggregate solubilization at higher β-CD concentrations. The study suggests that β-CD forms inclusion complexes with SDBS, thereby reducing its availability to interact with HEWL and mitigating aggregation, while promoting refolding. These findings underscore the potential of β-CD as a chemical chaperone in modulating protein aggregation, with implications for the formulation of therapeutic proteins and the understanding of protein misfolding diseases.
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BibTeX
@article{malik2026biphasic,
title = {{Biphasic Role of β-Cyclodextrin in Anionic Surfactant-induced Lysozyme Aggregation and Refolding}},
author = {Ajamaluddin Malik and Abdulaziz Alamri and Javed Masood Khan and Md Tabish Rehman and Mohammad Shamsul Ola and Hamza Odeibat},
journal = {Journal of Oleo Science},
year = {2026},
month = sep,
doi = {10.5650/jos.ess25193},
url = {https://www.jstage.jst.go.jp/article/jos/75/9/75_jos.ess25193/_article},
note = {CC BY},
}
RIS
TY - JOUR
TI - Biphasic Role of β-Cyclodextrin in Anionic Surfactant-induced Lysozyme Aggregation and Refolding
AU - Ajamaluddin Malik
AU - Abdulaziz Alamri
AU - Javed Masood Khan
AU - Md Tabish Rehman
AU - Mohammad Shamsul Ola
AU - Hamza Odeibat
PY - 2026
DA - 2026/09/01
JO - Journal of Oleo Science
DO - 10.5650/jos.ess25193
UR - https://www.jstage.jst.go.jp/article/jos/75/9/75_jos.ess25193/_article
AB - This study explores the role of β-cyclodextrin (β-CD) on the aggregation and refolding of hen egg white lysozyme (HEWL) induced by an anionic surfactant, i.e., sodium dodecylbenzenesulfonate (SDBS). Different biophysical techniques (Spectrophotometer, Flurometer, and Circular Dichroism) were employed to measure the conformational changes and aggregation propensity. UV-Vis spectroscopy revealed a biphasic turbidity response: initial β-CD concentrations (<0.4 mM) enhanced HEWL aggregation, whereas higher concentrations (>0.4 mM) solubilized the SDBS-induced aggregates, thereby restoring a native-like HEWL structure. Intrinsic fluorescence and circular dichroism analyses indicated that β-CD mitigated SDBS-induced structural disruptions, facilitating HEWL refolding. Thioflavin T assays confirmed the formation of amyloid-like fibrils in the SDBS-HEWL complex, which were solubilized upon addition of higher β-CD concentration, correlating with a decrease in turbidity,the regain of tertiary and secondary structure. Right-angle light scattering kinetic measurements supported these findings, showing rapid aggregate solubilization at higher β-CD concentrations. The study suggests that β-CD forms inclusion complexes with SDBS, thereby reducing its availability to interact with HEWL and mitigating aggregation, while promoting refolding. These findings underscore the potential of β-CD as a chemical chaperone in modulating protein aggregation, with implications for the formulation of therapeutic proteins and the understanding of protein misfolding diseases.
SN - 1347-3352
SN - 1345-8957
ER -