ArticleBiophysical journal2006
Assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 20 citations in OpenAlex.
- Adenosine Encapsulation and Characterization through Layer-by-Layer Assembly of Hydroxypropyl-Molecules (Basel, Switzerland) · 2024Article
- Solid-phase assisted refolding of carbonic anhydrase using beta-cyclodextrin-polyurethane polymer.The protein journal · 2008Article
- Dissecting the pretransitional conformational changes in aminoacylase I thermal denaturation.Biophysical journal · 2007Article
- Antichaperone activity of cyclodextrin derivatives.Doklady. Biochemistry and biophysicsArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclodextrin is a water-soluble circular oligosaccharide with a cylinder shape characterized by exterior hydrophilic rims and an interior hydrophobic cavity, which makes it an ideal additive to prevent proteins from aggregating during refolding. In this research, three hydroxypropyl cyclodextrins (HPCDs), HP-alpha-, beta-, and gamma-CD, were used to investigate the molecular mechanism of their effects on assisting aminoacylase refolding. The aggregation and reactivation experiments suggested that at moderate concentrations, HPCDs could suppress aggregation and assist aminoacylase refolding in a concentration-dependent manner, and HP-beta-CD was the most efficient of the three HPCDs. Low concentrations of HP-alpha-CD and high concentrations of HP-gamma-CD promoted off-pathway aggregation. Spectroscopic studies indicated that the hydrophobic exposure of the unstructured species in the refolded solutions was gradually reduced by the three HPCDs with the efficiency HP-beta-CD > HP-gamma-CD > HP-alpha-CD. Furthermore, the fast phase of aminoacylase reactivation was slowed down by the addition of 75 mM HP-beta- and gamma-CD, but no significant effect was observed for HP-alpha-CD. The dissimilarity in the effects of the three HPCDs suggested that the internal cavity size played a crucial role in their antiaggregation ability. Further analysis suggested that the observations might be much more complicated than expected because of the various types of interactions between cyclodextrins and proteins in addition to their ability to bind to protein aromatic residues.
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