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Chemical additives for protein refolding

  1. Top of page
  2. Chemical additives for protein refolding
  3. Single-molecule imaging of nanoparticle-DNA binding
  4. Quantitative assessment of collagen nanostructure

Yamaguchi et al., 2013, 8, 17–31.

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Are you at a loss as to what to do with inactive protein aggregates in your project? In laboratories and manufacturing settings, protein production from aggregates through refolding is a critical bottleneck. Rapid and inexpensive protein refolding is hindered by the fact that effective conditions tend to be protein-dependent and therefore difficult to select in a rational manner. In this issue, Yamaguchi and colleagues (Tokyo University, Tokyo, Japan) discuss synthetic refolding additives and describe the concepts underlying the development of chemical additives and chemical additive-based methods. This review contributes to the advancement of efficient refolding conditions in protein science and engineering fields, and additionally gives researchers in other discipline the incentive to start new studies in the development of a universal refolding method.

Single-molecule imaging of nanoparticle-DNA binding

  1. Top of page
  2. Chemical additives for protein refolding
  3. Single-molecule imaging of nanoparticle-DNA binding
  4. Quantitative assessment of collagen nanostructure

Li et al., Biotechnol. J. 2013, 8, 110–116.

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The interaction between nanoparticles (NPs) and DNA is an important research topic with broad applications and implications. On one hand, understanding the NP-DNA interaction is conducive to the rational design of nanobioconjugates for biomedical and therapeutic applications. On the other hand, in terms of safety concerns, NPs are likely to enter cells, and cause adverse effects on the stability and biological functions of DNA. In this issue, Li et al. (Georgia Tech, Atlanta, USA) employ atomic force microscopy to examine NP-DNA interactions at the single-molecule level. They observe that DNA conformation is changed after interacting with NPs, which may lead to subsequent changes in DNA function. This work is anticipated to benefit the future design of the NP-DNA bioconjugates and the evaluation of the genotoxicity of NPs.

Quantitative assessment of collagen nanostructure

  1. Top of page
  2. Chemical additives for protein refolding
  3. Single-molecule imaging of nanoparticle-DNA binding
  4. Quantitative assessment of collagen nanostructure

Erickson et al., Biotechnol. J. 2013, 8, 117–126.

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Type I collagen is the most abundant protein in mammals; it self-assembles into fibrils with a characteristic, nanoscale distribution of D-periodic gap/overlap spacing values. Recent studies have shown that this distribution changes with osteoporosis-related estrogen depletion, and with amino acid mutation (related to Osteogenesis imperfecta). In this issue, Erickson et al. (University of Michigan, Ann Arbor, USA) present the use of combined atomic force microscopy (AFM) imaging and two dimensional fast Fourier transform (2D FFT) analysis for the quantitative assessment of type I collagen fibril D-spacing. This method allows imaging and characterization of type I collagen in research areas such as tissue engineering, aging and disease assessment.