Single‐Molecule Determination of the Face‐Specific Adsorption of Amelogenin’s C‐Terminus on Hydroxyapatite

Friddle, Raymond W.; Battle, Keith; Trubetskoy, Vasily; Tao, Jinhui; Salter, E. Alan; Moradian‐Oldak, Janet; Yoreo, James J. De; Wierzbicki, Andrzej

doi:10.1002/ange.201100181

Cited by 10 publications

(11 citation statements)

References 31 publications

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“…The putative HAp interacting regions of amelogenin having the highest similarity, i.e., ADP1, ADP2 and ADP4, were synthesized chemically (see Supplementary Information ). For comparison, we also synthesized ADPs corresponding to the previously proposed putative mineral-binding regions near the C-terminus (ADP3, ADP6), 25 , 26 , 27 , 28 non-mineral interactive (e.g., low similarity score) regions (ADP5, ADP8) and finally ADP7, a peptide that included ADP1, ADP2 and ADP8 ( Figure 1e and Table 1 ). The HAp-binding affinities of these peptides were examined via QCM and their propensity to control formation of calcium phosphates were carried out via in vitro solution mineralization assays and ex vivo tooth re-mineralization experiments.…”

Section: Resultsmentioning

confidence: 99%

Cementomimetics—constructing a cementum-like biomineralized microlayer via amelogenin-derived peptides

et al. 2012

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Cementum is the outer-, mineralized-tissue covering the tooth root and an essential part of the system of periodontal tissue that anchors the tooth to the bone. Periodontal disease results from the destructive behavior of the host elicited by an infectious biofilm adhering to the tooth root and left untreated, may lead to tooth loss. We describe a novel protocol for identifying peptide sequences from native proteins with the potential to repair damaged dental tissues by controlling hydroxyapatite biomineralization. Using amelogenin as a case study and a bioinformatics scoring matrix, we identified regions within amelogenin that are shared with a set of hydroxyapatite-binding peptides (HABPs) previously selected by phage display. One 22-amino acid long peptide regions referred to as amelogenin-derived peptide 5 (ADP5) was shown to facilitate cell-free formation of a cementum-like hydroxyapatite mineral layer on demineralized human root dentin that, in turn, supported attachment of periodontal ligament cells in vitro. Our findings have several implications in peptide-assisted mineral formation that mimic biomineralization. By further elaborating the mechanism for protein control over the biomineral formed, we afford new insights into the evolution of protein–mineral interactions. By exploiting small peptide domains of native proteins, our understanding of structure–function relationships of biomineralizing proteins can be extended and these peptides can be utilized to engineer mineral formation. Finally, the cementomimetic layer formed by ADP5 has the potential clinical application to repair diseased root surfaces so as to promote the regeneration of periodontal tissues and thereby reduce the morbidity associated with tooth loss.

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Section: Resultsmentioning

confidence: 99%

Cementomimetics—constructing a cementum-like biomineralized microlayer via amelogenin-derived peptides

et al. 2012

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“…Finally, Friddle et al . (2011) used the adaptive biasing force simulation method, which is a technique based on thermodynamic integration to obtain free energy profiles using a biasing force, for the adsorption of a 12-mer C-terminal fragment of the amelogenin protein on various different crystal terminations of two different hydroxyapatite surfaces ((100) and (001)). By complementing AFM measurements with the free energy calculations, Friddle et al .…”

Section: Applications Of Free Energy Calculation Methods To Protein–smentioning

confidence: 99%

“…By complementing AFM measurements with the free energy calculations, Friddle et al . (2011) were able to predict the crystal termination of the hydroxyapatite surface used in experiments and identify the interactions governing the adsorption of the amelogenin peptide to it.…”

Section: Applications Of Free Energy Calculation Methods To Protein–smentioning

confidence: 99%

Modeling and simulation of protein–surface interactions: achievements and challenges

Ozboyaci

Kokh

Corni

et al. 2016

Quart. Rev. Biophys.

197

199

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Abstract. Understanding protein-inorganic surface interactions is central to the rational design of new tools in biomaterial sciences, nanobiotechnology and nanomedicine. Although a significant amount of experimental research on protein adsorption onto solid substrates has been reported, many aspects of the recognition and interaction mechanisms of biomolecules and inorganic surfaces are still unclear. Theoretical modeling and simulations provide complementary approaches for experimental studies, and they have been applied for exploring protein-surface binding mechanisms, the determinants of binding specificity towards different surfaces, as well as the thermodynamics and kinetics of adsorption. Although the general computational approaches employed to study the dynamics of proteins and materials are similar, the models and force-fields (FFs) used for describing the physical properties and interactions of material surfaces and biological molecules differ. In particular, FF and water models designed for use in biomolecular simulations are often not directly transferable to surface simulations and vice versa. The adsorption events span a wide range of time-and length-scales that vary from nanoseconds to days, and from nanometers to micrometers, respectively, rendering the use of multi-scale approaches unavoidable. Further, changes in the atomic structure of material surfaces that can lead to surface reconstruction, and in the structure of proteins that can result in complete denaturation of the adsorbed molecules, can create many intermediate structural and energetic states that complicate sampling. In this review, we address the challenges posed to theoretical and computational methods in achieving accurate descriptions of the physical, chemical and mechanical properties of protein-surface systems. In this context, we discuss the applicability of different modeling and simulation techniques ranging from quantum mechanics through all-atom molecular mechanics to coarse-grained approaches. We examine uses of different sampling methods, as well as free energy calculations. Furthermore, we review computational studies of protein-surface interactions and discuss the successes and limitations of current approaches.

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“…For data with M = 1, ..., 7, rupture force versus loading rate was analyzed using the Friddle–de Yoreo (FdY) model for M parallel bonds that can detach and reattach. 38 , 52 The FdY model has been used before to analyze the adhesion of proteins to substrates 53 , 54 of polymer to minerals 55 and of peptides to inorganic materials. 56 At low loading rates, the rapid (re)binding and unbinding leads to a constant rupture force, but at higher loading rates, the model recovers the known logarithmic loading-rate dependence for the case in which rebinding is neglected.…”

Section: Resultsmentioning

confidence: 99%

Self-Assembly of Elastin-like Polypeptide Brushes on Silica Surfaces and Nanoparticles

et al. 2021

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Control over the placement and activity of biomolecules on solid surfaces is a key challenge in bionanotechnology. While covalent approaches excel in performance, physical attachment approaches excel in ease of processing, which is equally important in many applications. We show how the precision of recombinant protein engineering can be harnessed to design and produce protein-based diblock polymers with a silica-binding and highly hydrophilic elastin-like domain that self-assembles on silica surfaces and nanoparticles to form stable polypeptide brushes that can be used as a scaffold for later biofunctionalization. From atomic force microscopy-based single-molecule force spectroscopy, we find that individual silica-binding peptides have high unbinding rates. Nevertheless, from quartz crystal microbalance measurements, we find that the self-assembled polypeptide brushes cannot easily be rinsed off. From atomic force microscopy imaging and bulk dynamic light scattering, we find that the binding to silica induces fibrillar self-assembly of the peptides. Hence, we conclude that the unexpected stability of these self-assembled polypeptide brushes is at least in part due to peptide–peptide interactions of the silica-binding blocks at the silica surface.

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Single‐Molecule Determination of the Face‐Specific Adsorption of Amelogenin’s C‐Terminus on Hydroxyapatite

Cited by 10 publications

References 31 publications

Cementomimetics—constructing a cementum-like biomineralized microlayer via amelogenin-derived peptides

Cementomimetics—constructing a cementum-like biomineralized microlayer via amelogenin-derived peptides

Modeling and simulation of protein–surface interactions: achievements and challenges

Self-Assembly of Elastin-like Polypeptide Brushes on Silica Surfaces and Nanoparticles

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