A review on protein oligomerization process

Liu, Shijie

doi:10.1007/s12541-015-0349-x

Cited by 16 publications

(11 citation statements)

References 208 publications

(224 reference statements)

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“…Moreover, some proteins adopt a quaternary structure, which implicates the association between protein subunits and their arrangements from dimers to oligomers. [ 26 , 27 ]. The self-association of proteins in different oligomeric states is mainly governed by nonbonded interactions such as the Van der Waals forces, hydrogen and ionic bonds and π–π interactions [ 28 ].…”

Section: Setting the Frame And Initial Considerationsmentioning

confidence: 99%

“…The self-association of proteins in different oligomeric states is mainly governed by nonbonded interactions such as the Van der Waals forces, hydrogen and ionic bonds and π–π interactions [ 28 ]. However, in some cases, the formation of specific disulfide bonds is critical for protein oligomerization [ 26 ]. The size of the self-associated superstructures could range from nm to µm.…”

Section: Setting the Frame And Initial Considerationsmentioning

confidence: 99%

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Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

2020

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The self-assembly of proteins is an essential process for a variety of cellular functions including cell respiration, mobility and division. On the other hand, protein or peptide misfolding and aggregation is related to the development of Parkinson’s disease and Alzheimer’s disease, among other aggregopathies. As a consequence, significant research efforts are directed towards the understanding of this process. In this review, we are focused on the use of UV-Visible Absorption Spectroscopy, Fluorescence Spectroscopy and Circular Dichroism to evaluate the self-organization of proteins and peptides in solution. These spectroscopic techniques are commonly available in most chemistry and biochemistry research laboratories, and together they are a powerful approach for initial as well as routine evaluation of protein and peptide self-assembly and aggregation under different environmental stimulus. Furthermore, these spectroscopic techniques are even suitable for studying complex systems like those in the food industry or pharmaceutical formulations, providing an overall idea of the folding, self-assembly, and aggregation processes, which is challenging to obtain with high-resolution methods. Here, we compiled and discussed selected examples, together with our results and those that helped us better to understand the process of protein and peptide aggregation. We put particular emphasis on the basic description of the methods as well as on the experimental considerations needed to obtain meaningful information, to help those who are just getting into this exciting area of research. Moreover, this review is particularly useful to those out of the field who would like to improve reproducibility in their cellular and biomedical experiments, especially while working with peptide and protein systems as an external stimulus. Our final aim is to show the power of these low-resolution techniques to improve our understanding of the self-assembly of peptides and proteins and translate this fundamental knowledge in biomedical research or food applications.

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Section: Setting the Frame And Initial Considerationsmentioning

confidence: 99%

Section: Setting the Frame And Initial Considerationsmentioning

confidence: 99%

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

2020

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“…A large part of the cellular proteins is oligomeric. Oligomerization of protein can often be a beneficial feature from the point of view of protein evolution and probably evolved by means of various mechanisms [5]. The main mechanism for the proper maturation and growth of mammalian oocytes is the organization by adequate storage of a large amount of mRNA and proteins.…”

Section: Discussionmentioning

confidence: 99%

Protein oligomerization is the biochemical process highly up-regulated in porcine oocytes before in vitro maturation (IVM)

Borys-Wójcik

Kocherova

Celichowski

et al. 2018

Medical Journal of Cell Biology

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A wide variety of mechanisms controlling oligomerization are observed. The dynamic nature of protein oligomerization is important for bioactivity control. The oocyte must undergo a series of changes to become a mature form before it can fully participate in the processes associated with its function as a female gamete. The growth of oocytes in the follicular environment is accompanied by surrounding somatic cumulus (CCs) and granulosa cells (GCs). It has been shown that oocytes tested before and after in vitro maturation (IVM) differ significantly in the transcriptomic and proteomic profiles. The aim of this study was to determine new proteomic markers for the oligomerization of porcine oocyte proteins that are associated with cell maturation competence. The Affymetrix microarray assay was performed to examine the gene expression profile associated with protein oligomerization in oocytes before and after IVM. In total, 12258 different transcriptomes were analyzed, of which 419 genes with lower expression in oocytes after IVM. We found 9 genes: GJA1, VCP, JUP, MIF, MAP3K1, INSR, ANGPTL4, EIF2AK3, DECR1, which were significantly down-regulated in oocytes after IVM (in vitro group) compared to oocytes analyzed before IVM (in vivo group). The higher expression of genes involved in the oligomerization of the protein before IVM indicates that they can be recognized as important markers of biological activation of proteins necessary for the further growth and development of pig embryos.

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“…The structural and functional aspects of protein oligomerization have acquired growing importance over the last two decades. Oligomerization is usually essential for proteins to execute their biological functions and thus is a phenomenon crucial in triggering various physiological pathways ( Hasimoto & Panchenko, 2010 ; Liu, 2015 ). The majority of protein oligomers forms through non-covalent weak associations, which can often lead to the assembly of subunits into metastable dimers or oligomers ( Liu, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

High-level expression and molecular characterization of a recombinant prolidase fromEscherichia coliNovaBlue

Wang

Chi

Lai

et al. 2018

PeerJ

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Long-term use of organophosphorus (OP) compounds has become an increasing global problem and a major threat to sustainability and human health. Prolidase is a proline-specific metallopeptidase that can offer an efficient option for the degradation of OP compounds. In this study, a full-length gene from Escherichia coli NovaBlue encoding a prolidase (EcPepQ) was amplified and cloned into the commercially-available vector pQE-30 to yield pQE-EcPepQ. The overexpressed enzyme was purified from the cell-free extract of isopropyl thio-β-D-galactoside IPTG-induced E. coli M15 (pQE-EcPepQ) cells by nickel-chelate chromatography. The molecular mass of EcPepQ was determined to be about 57 kDa by 12% sodium dodecyl sulfate–polyacrylamide gel electrophoresis and the result of size-exclusion chromatography demonstrated that the enzyme was mainly present in 25 mM Tris–HCl buffer (pH 8.0) as a dimeric form. The optimal conditions for EcPepQ activity were 60 °C, pH 8.0, and 0.1 mM Mn2+ ion. Kinetic analysis with Ala-Pro as the substrate showed that the Km and kcat values of EcPepQ were 8.8 mM and 926.5 ± 2.0 s−1, respectively. The thermal unfolding of EcPepQ followed a two-state process with one well-defined unfolding transition of 64.2 °C. Analysis of guanidine hydrochloride (GdnHCl)-induced denaturation by tryptophan emission fluorescence spectroscopy revealed that the enzyme had a [GdnHCl]0.5,N-U value of 1.98 M. The purified enzyme also exhibited some degree of tolerance to various water/organic co-solvents. Isopropanol and tetrahydrofuran were very detrimental to the enzymatic activity of EcPepQ; however, other more hydrophilic co-solvents, such as formamide, methanol, and ethylene glycol, were better tolerated. Eventually, the non-negative influence of some co-solvents on both catalytic activity and structural stability of EcPepQ allows to adjust the reaction conditions more suitable for EcPepQ-catalyzed bioprocess.

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A review on protein oligomerization process

Cited by 16 publications

References 208 publications

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

Protein oligomerization is the biochemical process highly up-regulated in porcine oocytes before in vitro maturation (IVM)

High-level expression and molecular characterization of a recombinant prolidase fromEscherichia coliNovaBlue

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