Literature DB >> 20365006

Model for amorphous aggregation processes.

Samuel D Stranks1, Heath Ecroyd, Steven Van Sluyter, Elizabeth J Waters, John A Carver, Lorenz von Smekal.   

Abstract

The amorphous aggregation of proteins is associated with many phenomena, ranging from the formation of protein wine haze to the development of cataract in the eye lens and the precipitation of recombinant proteins during their expression and purification. While much literature exists describing models for linear protein aggregation, such as amyloid fibril formation, there are few reports of models which address amorphous aggregation. Here, we propose a model to describe the amorphous aggregation of proteins which is also more widely applicable to other situations where a similar process occurs, such as in the formation of colloids and nanoclusters. As first applications of the model, we have tested it against experimental turbidimetry data of three proteins relevant to the wine industry and biochemistry, namely, thaumatin, a thaumatinlike protein, and alpha -lactalbumin. The model is very robust and describes amorphous experimental data to a high degree of accuracy. Details about the aggregation process, such as shape parameters of the aggregates and rate constants, can also be extracted.

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Year:  2009        PMID: 20365006     DOI: 10.1103/PhysRevE.80.051907

Source DB:  PubMed          Journal:  Phys Rev E Stat Nonlin Soft Matter Phys        ISSN: 1539-3755


  8 in total

1.  A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.

Authors:  Damien Hall; József Kardos; Herman Edskes; John A Carver; Yuji Goto
Journal:  FEBS Lett       Date:  2015-01-31       Impact factor: 4.124

2.  Experimental Model System to Study pH Shift-Induced Aggregation of Monoclonal Antibodies Under Controlled Conditions.

Authors:  Olubukayo-Opeyemi Oyetayo; Hans Kiefer
Journal:  Pharm Res       Date:  2016-02-29       Impact factor: 4.200

3.  Aggregation-phase diagrams of β2-microglobulin reveal temperature and salt effects on competitive formation of amyloids versus amorphous aggregates.

Authors:  Masayuki Adachi; Masahiro Noji; Masatomo So; Kenji Sasahara; József Kardos; Hironobu Naiki; Yuji Goto
Journal:  J Biol Chem       Date:  2018-08-03       Impact factor: 5.157

4.  Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.

Authors:  Yuichi Yoshimura; Yuxi Lin; Hisashi Yagi; Young-Ho Lee; Hiroki Kitayama; Kazumasa Sakurai; Masatomo So; Hirotsugu Ogi; Hironobu Naiki; Yuji Goto
Journal:  Proc Natl Acad Sci U S A       Date:  2012-08-20       Impact factor: 11.205

Review 5.  Measurement of amyloid formation by turbidity assay-seeing through the cloud.

Authors:  Ran Zhao; Masatomo So; Hendrik Maat; Nicholas J Ray; Fumio Arisaka; Yuji Goto; John A Carver; Damien Hall
Journal:  Biophys Rev       Date:  2016-11-23

6.  Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation.

Authors:  Yuanyuan Chen; Guxin Cui; Yuqi Cui; Dongru Chen; Huancai Lin
Journal:  AMB Express       Date:  2021-12-17       Impact factor: 3.298

7.  Rosin Surfactant QRMAE Can Be Utilized as an Amorphous Aggregate Inducer: A Case Study of Mammalian Serum Albumin.

Authors:  Mohd Ishtikhar; Tajjali Ilm Chandel; Aamir Ahmad; Mohd Sajid Ali; Hamad A Al-Lohadan; Ayman M Atta; Rizwan Hasan Khan
Journal:  PLoS One       Date:  2015-09-29       Impact factor: 3.240

8.  A mechanistic model for amorphous protein aggregation of immunoglobulin-like domains.

Authors:  Madeleine B Borgia; Adrian A Nickson; Jane Clarke; Michael J Hounslow
Journal:  J Am Chem Soc       Date:  2013-04-18       Impact factor: 15.419

  8 in total

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