Structure and Dynamics of Proteins Adsorbed to Biomaterial Interfaces

Drobny, Gary P.; Long, Joanna; Shaw, Wendy J.; Cotten, Myriam; Stayton, Pat

doi:10.1002/9780470034590.emrstm0540

Cited by 5 publications

(6 citation statements)

References 78 publications

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“…Previous solid state NMR measurements on fragments of statherin adsorbed to hydroxyapatite are reviewed elsewhere [81][82][83]. Investigation of full length surface-bound statherin was aimed initially at secondary structure elucidation of the protein's N-terminus [40].…”

Section: Nmr Structural Study Of Hap-bound Statherinmentioning

confidence: 99%

Solid state NMR studies of molecular recognition at protein–mineral interfaces

Goobes

Stayton

Drobny

2007

Progress in Nuclear Magnetic Resonance Spectroscopy

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Section: Nmr Structural Study Of Hap-bound Statherinmentioning

confidence: 99%

Solid state NMR studies of molecular recognition at protein–mineral interfaces

Goobes

Stayton

Drobny

2007

Progress in Nuclear Magnetic Resonance Spectroscopy

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“…Recent studies rather suggest that protein adsorption can result in a decrease of the adsorbed protein dynamics. 54,55 Using elastic and inelastic neutron scattering experiments, we showed that myoglobin adsorption on SNPs leads to a decrease of protein flexibility and to a depletion in low frequency modes, suggesting that the structural loss of the adsorbed protein may not be the entropic driving force of adsorption. 47 The aim of this study is to investigate the modifications of hemoglobin structure and activity after adsorption on SNPs in connection with our results on the dynamics of adsorbed myoglobin.…”

Section: Introductionmentioning

confidence: 97%

“…However, few experimental studies have been performed to investigate protein dynamics on surfaces despite its importance in biological processes. Recent studies rather suggest that protein adsorption can result in a decrease of the adsorbed protein dynamics 54,55 . Using elastic and inelastic neutron scattering experiments, we showed that myoglobin adsorption on SNPs leads to a decrease of protein flexibility and to a depletion in low frequency modes, suggesting that the structural loss of the adsorbed protein may not be the entropic driving force of adsorption 47 .…”

Section: Introductionmentioning

confidence: 99%

Structure and Function of Adsorbed Hemoglobin on Silica Nanoparticles: Relationship between the Adsorption Process and the Oxygen Binding Properties

et al. 2017

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The connection between the mechanisms of protein adsorption on nanoparticles and the structural and functional properties of the adsorbed protein often remains unclear. We investigate porcine hemoglobin adsorption on silica nanoparticles, and we analyze the structural and functional modifications of adsorbed hemoglobin by UV-vis spectrophotometry, circular dichroism, and oxygen binding measurement. The structural analysis of adsorbed hemoglobin on silica nanoparticles reveals a significant loss of secondary structure and a preservation of the heme electronic structure. However, adsorbed hemoglobin retains its quaternary structure and exhibits an enhanced oxygen affinity with cooperative binding. Moreover, the structural and functional modifications are fully reversible after complete desorption from silica nanoparticles at pH 8.7. The tunable adsorption and desorption of hemoglobin on SNPs with pH change, and the full control of hemoglobin activity by pH, temperature, and the addition of inorganic phosphate effectors opens the way to an interesting system whereby protein adsorption on nanoparticles can allow for full control over hemoglobin oxygen binding activity. Our results suggest that adsorption of hemoglobin on silica nanoparticles leads to a new structural, functional, and dynamic state with full reversibility in a way that significantly differs from protein denaturation.

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“…Protein-crystal interactions play a fundamental role in many biological processes such as biomineralization [1–4]. For example, bone is a natural protein-crystal composite containing nanoscopic bone apatite crystals highly organized within a fibrillar protein extracellular matrix (ECM) that consists predominantly of collagen I [5].…”

Section: Introductionmentioning

confidence: 99%

Protein-crystal interface mediates cell adhesion and proangiogenic secretion

Weisi

Brian

et al. 2017

Biomaterials

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The nanoscale materials properties of bone apatite crystals have been implicated in breast cancer bone metastasis and their interactions with extracellular matrix proteins are likely involved. In this study, we used geologic hydroxyapatite (HAP, Ca10(PO4)6(OH)2), closely related to bone apatite, to investigate how HAP surface chemistry and nano/microscale topography individually influence the crystal-protein interface, and how the altered protein deposition impacts subsequent breast cancer cell activities. We first utilized Förster resonance energy transfer (FRET) to assess the molecular conformation of fibronectin (Fn), a major extracellular matrix protein upregulated in cancer, when it adsorbed onto HAP facets. Our analysis reveals that both low surface charge density and nanoscale roughness of HAP facets individually contributed to molecular unfolding of Fn. We next quantified cell adhesion and secretion on Fn-coated HAP facets using MDA-MB-231 breast cancer cells. Our data show elevated proangiogenic and proinflammatory secretions associated with more unfolded Fn adsorbed onto nano-rough HAP facets with low surface charge density. These findings not only deconvolute the roles of crystal surface chemistry and topography in interfacial protein deposition but also enhance our knowledge of protein-mediated breast cancer cell interactions with apatite, which may be implicated in tumor growth and bone metastasis.

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Structure and Dynamics of Proteins Adsorbed to Biomaterial Interfaces

Cited by 5 publications

References 78 publications

Solid state NMR studies of molecular recognition at protein–mineral interfaces

Solid state NMR studies of molecular recognition at protein–mineral interfaces

Structure and Function of Adsorbed Hemoglobin on Silica Nanoparticles: Relationship between the Adsorption Process and the Oxygen Binding Properties

Protein-crystal interface mediates cell adhesion and proangiogenic secretion

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