The Two‐Step Assemblies of Basic‐Amino‐Acid‐Rich Peptide with a Highly Charged Polyoxometalate

Zhang, Teng; Li, Hongwei; Wu, Yuqing; Wang, Yizhan; Wu, Lixin

doi:10.1002/chem.201501243

Cited by 23 publications

(22 citation statements)

References 38 publications

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“…The FA1 site was stabilized by a host of hydrogen bonds from positively charged amino acid residues of HSA. These types of interactions have been previously proposed to drive the association of POMs with biomolecules. − For instance, Arg117, Arg186, and Arg428 formed multiple hydrogen bonds through interactions between their amine protons and the negatively charged oxygen cage of ZrK (Figure c). Additionally, positively charged Lys190 and Lys519 residues associated through hydrogen bonding with the surface of ZrK (Figure c,d).…”

Section: Resultsmentioning

confidence: 88%

Investigating Polyoxometalate–Protein Interactions at Chemically Distinct Binding Sites

et al. 2018

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In this study, a combined molecular docking (rigid and flexible) and all-atom molecular dynamics simulations technique have been employed to investigate interactions of 1:1 Zr-containing Keggin polyoxometalate (ZrK) with four chemically distinct cleavage sites [Arg114-Leu115 (site 1), Ala257-Asp258 (site 2), Lys313-Asp314 (site 3), and Cys392-Glu393 (site 4)] of human serum albumin (HSA). The ZrK-HSA complexations were analyzed using electrostatic potentials, the chemical nature of amino acid residues, binding free energies, and secondary structures as parameters. They suggested that ZrK binds in a rather distinct manner to different cleavage sites, and its association was dominated by hydrogen bonding, both direct and solvent mediated, and electrostatic interactions, as suggested experimentally. The computed binding free interaction energies (-57.5, -24.2, -50.8, and -91.2 kJ/mol for sites 1, 2, 3, and 4, respectively) predicted the existence of one major binding site (site 4) and three minor binding sites (site 1, site 2, and site 3). The strong exothermicity of the binding was also supported by isothermal calorimetry experiments. Additionally, the binding of ZrK did not alter the overall α-helical secondary structure of HSA, which was in line with experimental observation. Furthermore, hydrolysis of the peptide bonds of the substrate was found to retain its overall structure. These results have provided a deeper understanding of the complex ZrK interactions with proteins, and they will lead to the design of the next generation of catalytically active polyoxometalates with improved hydrolytic activities.

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Section: Resultsmentioning

confidence: 88%

Investigating Polyoxometalate–Protein Interactions at Chemically Distinct Binding Sites

et al. 2018

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“…The incubation for 24 h or longer did not lead to precipitation, but maintained a stabilized aggregate with a slight increase in size to 82 nm ( Figure 2 D). As already shown, the negatively charged POMs bind with some peptides containing basic residues through electrostatic interaction and hydrogen bonding [ 31 , 32 ]. The non-specific interaction can also induce the combination of the [Mo 132 ] cluster bearing 42 negative charges with L1-p, causing the formation of larger assemblies or aggregates.…”

Section: Resultsmentioning

confidence: 99%

A Visual Discrimination of Existing States of Virus Capsid Protein by a Giant Molybdate Cluster

Xue

Wei

et al. 2022

Nanomaterials

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We report a unique phenomenon, the opposite color response of a giant polyoxometalate, (NH4)42[Mo132O372(CHCOO)30] (H2O)72 ([Mo132]), to the existing states of human papillomavirus (HPV) major capsid protein, L1-pentamer (L1-p), and virus-like particles (VLPs). The color responses originate from the different assembly forms between [Mo132] and the capsid protein. The latter were inspected and separated by using CsCl gradient centrifugation, and validated in detail by sodium dodecyl sulfate-polyacrylamide gel-electrophoresis (SDS-PAGE), dynamic light scattering (DLS), and transmission electron microscopy (TEM) imaging. Furthermore, the intrinsic mechanisms were investigated in-depth by using XPS-based semi-quantitative analysis and well-designed peptides, revealing the critical points of L1 that determine the charge–transfer ratio between Mo(V) to Mo(VI), and consequently, the levels of [Mo132] hypochromic in different assemblies. Such a unique phenomenon is significant as it supplies a colorimetry approach to distinguish the existing states of the HPV capsid protein and would be significant in the quality assay of the HPV vaccine and existing states of other viruses in the future.

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“…The incubation for 24 h or longer time does not lead to any precipitation but maintains at a stabilized aggregate with a slight increase in size to 82 nm (Figure 2D). As have been demonstrated the negatively charged POMs bind with some peptides containing basic residues through electrostatic interaction and hydrogen bonding, 31,32 the non-speci c interaction can also induce the combination of [Mo 132 ] cluster bearing 42 negative charges with L1-p, causing the formation of larger assemblies or aggregates.…”

Section: Resultsmentioning

confidence: 99%

A Visual Discrimination of Existing States of Virus Capsid Protein by a Giant Molybdate Cluster

Xue,

Wei,

et al. 2021

Preprint

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This study reports a unique phenomenon, the opposite color response of a giant polyoxometalate, (NH4)42[Mo132O372(CHCOO)30] (H2O)72 ([Mo132]), to the existing states of human papillomavirus (HPV) major capsid protein, L1-pentamer (L1-p) and virus-like particles (VLPs). The color responses originate from the different assembly forms between [Mo132] and the capsid protein, which were inspected and separated by using CsCl gradient centrifugation, and validated in detail by sodium dodecyl sulfate polyacrylamide gel-electrophoresis (SDS-PAGE), dynamic light scattering (DLS) and transmission electron microscopy (TEM) images. The intrinsic mechanism difference between them were investigated in depth by using the XPS-based semi-quantitative analysis and the well designed peptides, which reveal the key points of L1 determining the charge-transfer ratio between Mo(V) to Mo(VI), and consequently the levels of [Mo132] hypochromicity in different assemblies. Such unique phenomenon is significant as it supplies a colorimetry approach to directly distinguish the existing states of HPV capsid protein and would be significant in the quality assay of HPV vaccine and existing states of other virus in future.

show abstract

The Two‐Step Assemblies of Basic‐Amino‐Acid‐Rich Peptide with a Highly Charged Polyoxometalate

Cited by 23 publications

References 38 publications

Investigating Polyoxometalate–Protein Interactions at Chemically Distinct Binding Sites

Investigating Polyoxometalate–Protein Interactions at Chemically Distinct Binding Sites

A Visual Discrimination of Existing States of Virus Capsid Protein by a Giant Molybdate Cluster

A Visual Discrimination of Existing States of Virus Capsid Protein by a Giant Molybdate Cluster

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