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Bradley D. Olsen - One of the best experts on this subject based on the ideXlab platform.
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improved ordering in low molecular weight protein polymer conjugates through oligomerization of the protein block
Biomacromolecules, 2018Co-Authors: Justin M Paloni, Eric Miller, Hadley D Sikes, Bradley D. OlsenAbstract:The self-assembly of protein-polymer conjugates incorporating oligomers of a small, engineered high-affinity binding protein, rcSso7d.SA, is studied to determine the effect of protein oligomerization on nanoscale ordering. Oligomerization enables a systematic increase in the protein molar mass without changing its overall folded structure, leading to a higher driving force for self-assembly into well-ordered structures. Though conjugates of monomeric rcSso7d.SA are found to only exist in disordered states, oligomers of this protein linked to a poly( N-isopropylacrylamide) (PNIPAM) block self-assemble into lamellar nanostructures. Conjugates of trimeric and tetrameric rcSso7d.SA are observed to produce the strongest ordering in concentrated solution, displaying birefringent lamellae at concentrations as low as 40 wt %. In highly concentrated solution, the oligomeric rcSso7d.SA-PNIPAM block copolymers exhibit ordering and domain spacing trends atypical from that of most block copolymers. Fluorescent binding assays indicate that oligomerized protein blocks retain binding functionality and exhibit limits of detection up to three times lower than that of surface-immobilized protein sensors. Therefore, oligomerization of the protein block in these block copolymers serves as an effective method to improve both nanoscale ordering and biosensing capabilities.
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the nature of protein interactions governing globular protein polymer block copolymer self assembly
Biomacromolecules, 2014Co-Authors: Carla S Thomas, Gabriel Sanoja, Chimdimma U Okwara, Dongsook Chang, Bradley D. OlsenAbstract:The effects of protein surface potential on the self-assembly of protein–polymer block copolymers are investigated in globular proteins with controlled shape through two approaches: comparison of self-assembly of mCherry-poly(N-isopropylacrylamide) (PNIPAM) bioconjugates with structurally homologous enhanced green fluorescent protein (EGFP)-PNIPAM bioconjugates, and mutants of mCherry with altered electrostatic patchiness. Despite large changes in amino acid sequence, the temperature–concentration phase diagrams of EGFP-PNIPAM and mCherry-PNIPAM conjugates have similar phase transition concentrations. Both materials form identical phases at two different coil fractions below the PNIPAM thermal transition temperature and in the bulk. However, at temperatures above the thermoresponsive transition, mCherry conjugates form hexagonal phases at high concentrations while EGFP conjugates form a disordered micellar phase. At lower concentration, mCherry shows a two-phase region while EGFP forms homogeneous disorde...
Jie Wang - One of the best experts on this subject based on the ideXlab platform.
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ca2 induced self assembly of bombyx mori silk sericin into a nanofibrous network like protein matrix for directing controlled nucleation of hydroxylapatite nano needles
Journal of Materials Chemistry B, 2015Co-Authors: Mingying Yang, Guanshan Zhou, Yajun Shuai, Jie WangAbstract:Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within the self-assembled protein matrix. Mimicking this process is a promising approach to the production of bone-like protein/mineral nanocomposites for bone repair and regeneration. Towards the goal of fabricating such nanocomposites from sericin, a protein spun by Bombyx mori (B. mori) silkworm, and bone mineral HAP, for the first time we investigated the chemical mechanism underpinning the synergistic processes of the conformational change/self-assembly of B. mori sericin (BS) as well as the nucleation of HAP on the resultant self-assembled BS matrix. We found that BS, rich in anionic amino acid residues, could bind Ca2+ ions from the HAP precursor solution through electrostatic attraction. The Ca2+ binding drove the conformational change of BS from random coils into β-sheets and its concomitant self-assembly into the interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembled BS matrix grew preferentially along their crystallographic c-axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembled BS matrix were subsequently aggregated into globules, probably driven by the hydrogen bonding between CO groups of BS and O–H groups of HAP nano-needles. The present work sheds light on the chemical mechanisms of BS self-assembly and the controlled mineralization directed by the self-assembled matrix. We also found that the resultant nanocomposites could promote the osteogenic differentiation of human bone marrow-derived mesenchymal stem cells. Thus our work also generates a biomimetic approach to bone-like silk protein/mineral nanocomposite scaffolds that can find potential applications in bone repair and regeneration.
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ca2 induced self assembly of bombyx mori silk sericin into a nanofibrous network like protein matrix for directing controlled nucleation of hydroxylapatite nano needles
Journal of Materials Chemistry B, 2015Co-Authors: Mingying Yang, Guanshan Zhou, Yajun Shuai, Jie Wang, Liangjun Zhu, Chuanbin MaoAbstract:Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within self-assembled protein matrix. Mimicking this process is a promising approach to the production of bone-like protein/mineral nanocomposites for bone repair and regeneration. Towards the goal of fabricating such nanocomposites from sericin, a protein spun by Bombyx mori (B.mori) silkworm, and bone mineral HAP, for the first time we investigated the chemical mechanism underpinning the synergistic processes of the conformational change/self-assembly of B.mori sericin ( BS ) as well as the nucleation of HAP on the resultant self-assembled BS matrix. We found that BS , rich in anionic amino acid residues, could bind Ca2+ ions from the HAP precursor solution through electrostatic attraction. The Ca2+binding drove the conformational change of BS from random coils into β-sheets and its concomitant self-assembly into interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembled BS matrix grew preferentially along their crystallographic c-axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembled BS matrix were subsequently aggregated into globules, probably driven by the hydrogen bonding between C=O groups of BS and O-H groups of HAP nano-needles. The present work sheds light on the chemical mechanisms of BS self-assembly and the controlled mineralization directed by the self-assembled matrix. We also found that the resultant nanocomposites could promote the osteogenic differentiation of human bone marrow-derived mesenchymal stem cells. Thus our work also generates a biomimetic approach to bone-like silk protein/mineral nanocomposite scaffolds that can find potential applications in bone repair and regeneration.
Mingying Yang - One of the best experts on this subject based on the ideXlab platform.
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ca2 induced self assembly of bombyx mori silk sericin into a nanofibrous network like protein matrix for directing controlled nucleation of hydroxylapatite nano needles
Journal of Materials Chemistry B, 2015Co-Authors: Mingying Yang, Guanshan Zhou, Yajun Shuai, Jie WangAbstract:Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within the self-assembled protein matrix. Mimicking this process is a promising approach to the production of bone-like protein/mineral nanocomposites for bone repair and regeneration. Towards the goal of fabricating such nanocomposites from sericin, a protein spun by Bombyx mori (B. mori) silkworm, and bone mineral HAP, for the first time we investigated the chemical mechanism underpinning the synergistic processes of the conformational change/self-assembly of B. mori sericin (BS) as well as the nucleation of HAP on the resultant self-assembled BS matrix. We found that BS, rich in anionic amino acid residues, could bind Ca2+ ions from the HAP precursor solution through electrostatic attraction. The Ca2+ binding drove the conformational change of BS from random coils into β-sheets and its concomitant self-assembly into the interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembled BS matrix grew preferentially along their crystallographic c-axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembled BS matrix were subsequently aggregated into globules, probably driven by the hydrogen bonding between CO groups of BS and O–H groups of HAP nano-needles. The present work sheds light on the chemical mechanisms of BS self-assembly and the controlled mineralization directed by the self-assembled matrix. We also found that the resultant nanocomposites could promote the osteogenic differentiation of human bone marrow-derived mesenchymal stem cells. Thus our work also generates a biomimetic approach to bone-like silk protein/mineral nanocomposite scaffolds that can find potential applications in bone repair and regeneration.
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ca2 induced self assembly of bombyx mori silk sericin into a nanofibrous network like protein matrix for directing controlled nucleation of hydroxylapatite nano needles
Journal of Materials Chemistry B, 2015Co-Authors: Mingying Yang, Guanshan Zhou, Yajun Shuai, Jie Wang, Liangjun Zhu, Chuanbin MaoAbstract:Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within self-assembled protein matrix. Mimicking this process is a promising approach to the production of bone-like protein/mineral nanocomposites for bone repair and regeneration. Towards the goal of fabricating such nanocomposites from sericin, a protein spun by Bombyx mori (B.mori) silkworm, and bone mineral HAP, for the first time we investigated the chemical mechanism underpinning the synergistic processes of the conformational change/self-assembly of B.mori sericin ( BS ) as well as the nucleation of HAP on the resultant self-assembled BS matrix. We found that BS , rich in anionic amino acid residues, could bind Ca2+ ions from the HAP precursor solution through electrostatic attraction. The Ca2+binding drove the conformational change of BS from random coils into β-sheets and its concomitant self-assembly into interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembled BS matrix grew preferentially along their crystallographic c-axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembled BS matrix were subsequently aggregated into globules, probably driven by the hydrogen bonding between C=O groups of BS and O-H groups of HAP nano-needles. The present work sheds light on the chemical mechanisms of BS self-assembly and the controlled mineralization directed by the self-assembled matrix. We also found that the resultant nanocomposites could promote the osteogenic differentiation of human bone marrow-derived mesenchymal stem cells. Thus our work also generates a biomimetic approach to bone-like silk protein/mineral nanocomposite scaffolds that can find potential applications in bone repair and regeneration.
John L Foster - One of the best experts on this subject based on the ideXlab platform.
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self association of the lentivirus protein nef
Retrovirology, 2010Co-Authors: Youn Tae Kwak, Brenda Temple, Alexa Raney, Lillian S Kuo, Sarah J Denial, Victor J Garcia, John L FosterAbstract:Background The HIV-1 pathogenic factor, Nef, is a multifunctional protein present in the cytosol and on membranes of infected cells. It has been proposed that a spatial and temporal regulation of the conformation of Nef sequentially matches Nef's multiple functions to the process of virion production. Further, it has been suggested that dimerization is required for multiple Nef activities. A dimerization interface has been proposed based on intermolecular contacts between Nefs within hexagonal Nef/FynSH3 crystals. The proposed dimerization interface consists of the hydrophobic B-helix and flanking salt bridges between R105 and D123. Here, we test whether Nef self-association is mediated by this interface and address the overall significance of oligomerization.
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self association of the lentivirus protein nef
Retrovirology, 2010Co-Authors: Youn Tae Kwak, Brenda Temple, Alexa Raney, Lillian S Kuo, Sarah J Denial, Victor J Garcia, John L FosterAbstract:The HIV-1 pathogenic factor, Nef, is a multifunctional protein present in the cytosol and on membranes of infected cells. It has been proposed that a spatial and temporal regulation of the conformation of Nef sequentially matches Nef's multiple functions to the process of virion production. Further, it has been suggested that dimerization is required for multiple Nef activities. A dimerization interface has been proposed based on intermolecular contacts between Nefs within hexagonal Nef/FynSH3 crystals. The proposed dimerization interface consists of the hydrophobic B-helix and flanking salt bridges between R105 and D123. Here, we test whether Nef self-association is mediated by this interface and address the overall significance of oligomerization. By co-immunoprecipitation assays, we demonstrated that HIV-1Nef exists as monomers and oligomers with about half of the Nef protomers oligomerized. Nef oligomers were found to be present in the cytosol and on membranes. Removal of the myristate did not enhance the oligomerization of soluble Nef. Also, SIVNef oligomerizes despite lacking a dimerization interface functionally homologous to that proposed for HIV-1Nef. Moreover, HIV-1Nef and SIVNef form hetero-oligomers demonstrating the existence of homologous oligomerization interfaces that are distinct from that previously proposed (R105-D123). Intracellular cross-linking by formaldehyde confirmed that SF2Nef dimers are present in intact cells, but surprisingly self-association was dependent on R105, but not D123. SIVMAC239Nef can be cross-linked at its only cysteine, C55, and SF2Nef is also cross-linked, but at C206 instead of C55, suggesting that Nefs exhibit multiple dimeric structures. ClusPro dimerization analysis of HIV-1Nef homodimers and HIV-1Nef/SIVNef heterodimers identified a new potential dimerization interface, including a dibasic motif at R105-R106 and a six amino acid hydrophobic surface. We have demonstrated significant levels of intracellular Nef oligomers by immunoprecipitation from cellular extracts. However, our results are contrary to the identification of salt bridges between R105 and D123 as necessary for self-association. Importantly, binding between HIV-1Nef and SIVNef demonstrates evolutionary conservation and therefore significant function(s) for oligomerization. Based on modeling studies of Nef self-association, we propose a new dimerization interface. Finally, our findings support a stochastic model of Nef function with a dispersed intracellular distribution of Nef oligomers.
Chuanbin Mao - One of the best experts on this subject based on the ideXlab platform.
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ca2 induced self assembly of bombyx mori silk sericin into a nanofibrous network like protein matrix for directing controlled nucleation of hydroxylapatite nano needles
Journal of Materials Chemistry B, 2015Co-Authors: Mingying Yang, Guanshan Zhou, Yajun Shuai, Jie Wang, Liangjun Zhu, Chuanbin MaoAbstract:Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within self-assembled protein matrix. Mimicking this process is a promising approach to the production of bone-like protein/mineral nanocomposites for bone repair and regeneration. Towards the goal of fabricating such nanocomposites from sericin, a protein spun by Bombyx mori (B.mori) silkworm, and bone mineral HAP, for the first time we investigated the chemical mechanism underpinning the synergistic processes of the conformational change/self-assembly of B.mori sericin ( BS ) as well as the nucleation of HAP on the resultant self-assembled BS matrix. We found that BS , rich in anionic amino acid residues, could bind Ca2+ ions from the HAP precursor solution through electrostatic attraction. The Ca2+binding drove the conformational change of BS from random coils into β-sheets and its concomitant self-assembly into interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembled BS matrix grew preferentially along their crystallographic c-axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembled BS matrix were subsequently aggregated into globules, probably driven by the hydrogen bonding between C=O groups of BS and O-H groups of HAP nano-needles. The present work sheds light on the chemical mechanisms of BS self-assembly and the controlled mineralization directed by the self-assembled matrix. We also found that the resultant nanocomposites could promote the osteogenic differentiation of human bone marrow-derived mesenchymal stem cells. Thus our work also generates a biomimetic approach to bone-like silk protein/mineral nanocomposite scaffolds that can find potential applications in bone repair and regeneration.