Endothelialization of Titanium Surfaces

Meyers, Steven R.; Hamilton, P. B.; Walsh, Elisabeth B.; Kenan, Daniel J.; Grinstaff, Mark W.

doi:10.1002/adma.200700029

Cited by 44 publications

(48 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…27 We have also previously reported peptides that bind metals, metal oxides, and plastics. 23,34,54 Both Sanghvi et al and Meyer et al individually described bimodular RGD peptides that promoted cell adhesion to polypyrrole and Ti metal, respectively. 34,46,47 Application of IFBMs to degradable biomaterials such as PGA has not been previously reported.…”

Section: Discussionmentioning

confidence: 97%

“…In this fashion, these peptides create an interface that allows for appropriate biological interactions with inert materials. Our previous research focused on using bifunctional resulting peptides to regulate the interactions that occurred at the biological-material interface including: promotion of surface cellularization, 34 suppression of apoptosis, 36 prevention of fouling, 23,24 and, more recently, release of a therapeutic from a surface. 35 In this report, we have approached the problem of poor biological activity of PGA fibers by developing a modular IFBM peptide that is capable of binding to PGA and modifying its surface to provide biological cues that direct endothelial cell adhesion, spreading, cytoskeletal reorganization, and focal adhesion plaque formation.…”

Section: Discussionmentioning

confidence: 99%

“…23,24,[34][35][36]54 These bifunctional, two-domain peptide coatings must recognize and bind both the inert surface through non-covalent physisorption, while also providing a mechanism to interact with the surrounding biology. In this fashion, these peptides create an interface that allows for appropriate biological interactions with inert materials.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

et al. 2010

View full text Add to dashboard Cite

Resorbable scaffolds such as polyglycolic acid (PGA) are employed in a number of clinical and tissue engineering applications owing to their desirable property of allowing remodeling to form native tissue over time. However, native PGA does not promote endothelial cell adhesion. Here we describe a novel treatment with hetero-bifunctional peptide linkers, termed "interfacial biomaterials" (IFBMs), which are used to alter the surface of PGA to provide appropriate biological cues. IFBMs couple an affinity peptide for the material with a biologically active peptide that promotes desired cellular responses. One such PGA affinity peptide was coupled to the integrin binding domain, Arg-Gly-Asp (RGD), to build a chemically synthesized bimodular 27 amino acid peptide that mediated interactions between PGA and integrin receptors on endothelial cells. Quartz crystal microbalance with dissipation monitoring (QCMD) was used to determine the association constant (K (A) 1 x 10(7) M(-1)) and surface thickness (~3.5 nm). Cell binding studies indicated that IFBM efficiently mediated adhesion, spreading, and cytoskeletal organization of endothelial cells on PGA in an integrin-dependent manner. We show that the IFBM peptide promotes a 200% increase in endothelial cell binding to PGA as well as 70-120% increase in cell spreading from 30 to 60 minutes after plating.

show abstract

Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

et al. 2010

View full text Add to dashboard Cite

show abstract

“…5,17 Therefore, the investigation of entire peptide chains in contact with inorganic surfaces is a critical component in advancing our understanding. 26 The tripeptide motif RGD and its interaction with titania surfaces has been of particular interest, [27][28][29][30][31][32][33] while others have sought to isolate and identify TiO2-binding peptides using biocombinatorial techniques to gain a deeper understanding of which peptide characteristics can confer strong titania-binding affinity. 32,[34][35][36][37] A crucial next step in advancing our understanding is the careful characterization of the adsorption of materials-binding peptides at aqueous titania interfaces.…”

Section: Introductionmentioning

confidence: 99%

“…26 The tripeptide motif RGD and its interaction with titania surfaces has been of particular interest, [27][28][29][30][31][32][33] while others have sought to isolate and identify TiO2-binding peptides using biocombinatorial techniques to gain a deeper understanding of which peptide characteristics can confer strong titania-binding affinity. 32,[34][35][36][37] A crucial next step in advancing our understanding is the careful characterization of the adsorption of materials-binding peptides at aqueous titania interfaces. [36][37][39][40][41][42][43] Of particular note is the work of Yazici et al 36 who used quartz crystal microbalance (QCM) measurements to determine the binding free energy of three sequences; two "strong-binders", RPRGNRGRERGL and SRPNGYGGSESS, with Gads= -34.5 and -38.5 kJ mol -1 respectively and one "weak-binder", VGRVTSPRPQGR, with Gads= -27.6 kJ mol -1 , identified from cell-surface display screening experiments.…”

Section: Introductionmentioning

confidence: 99%

Aqueous Peptide–TiO₂ Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

Sultan

Westcott

Hughes

et al. 2016

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

A major barrier to the systematic improvement of biomimetic peptide-mediated strategies for the controlled growth of inorganic nanomaterials in environmentally benign conditions lies in the lack of clear conceptual connections between the sequence of the peptide and its surface binding affinity, with binding being facilitated by non-covalent interactions. Peptide conformation, both in the adsorbed and non-adsorbed state, is the key relationship that connects peptide-materials binding with peptide sequence. Here, we combine experimental peptide-titania binding characterization with state-of-the-art conformational sampling via molecular simulations to elucidate these structure/binding relationships for two very different titania-binding peptide sequences. The two sequences (Ti-1: QPYLFATDSLIK and Ti-2:GHTHYHAVRTQT) differ in their overall hydropathy, yet via quartz-crystal microbalance measurements and predictions from molecular simulations, we show these sequences both support very similar, strong titania-binding affinities. Our molecular simulations reveal that the two sequences exhibit profoundly different modes of surface binding, with Ti-1 acting as an entropically-driven binder while Ti-2 behaves as an enthalpically-driven binder. The integrated approach presented here provides a rational basis for peptide sequence engineering to achieve the in-situ growth and organization of titania nanostructures in aqueous media and for the design of sequences suitable for a range of technological applications that involve the interface between titania and biomolecules.3

show abstract

Enzymatic Release of a Surface‐Adsorbed RGD Therapeutic from a Cleavable Peptide Anchor

2008

View full text Add to dashboard Cite

Implantation of a polymeric, ceramic, or metallic implant will unavoidably activate a response from the surrounding tissue. [1] Means to attenuate this inflammatory response at the implant site are of significant interest and currently include strategies based on surface morphology, chemical modification, or drug delivery. This response is particularly evident at the site of stent deployment, where the overproliferation of smooth muscle cells can lead to restenosis-a re-narrowing of the lumen.[2] Drug-eluting stents (DES) were introduced to decrease the rate and severity of this neointimal formation through passive diffusion of a drug physically entrapped in a nondegradable polymer coating over a metal framework. However, recent studies have expressed concern over the widespread use of DES owing to their increased late-thrombotic potential of two to three times the rates for a traditional bare metal stent. [3] This clinical outcome is likely due to delayed healing and endothelium regeneration as a result of the polymer coating (e.g., poly(styrene-b-isobutyl-b-styrene)) and the delivery of non-phenotype-specific antimitotic/antiproliferative drugs (e.g., sirolimus and paclitaxel). With the goal of improving implant performance through appropriate interactions with the surrounding biology, we previously reported the use of implant-specific peptide coatings to prevent nonspecific surface biofouling and to promote a pro-healing response through increasing cell adhesion and spreading.[4] Herein we report a third approach whereby a surface-adsorbed therapeutic is enzymatically released, resulting in drug elution (Figure 1).Engineering of an enzymatic recognition site into a material is an elegant approach to promote active degradation and has been used successfully with hydrogels, microspheres, bioplexes, and interpenetrating networks, [5] as well as for evaluating enzyme kinetics in the degradation of peptides on surfaces. [6] The enzymatic release of an adsorbed or tethered therapeutic from an implant surface is an exciting idea which would likely be of interest for many medical devices, including stents. Current stenting applications rely on passive drug entrapment and diffusion, and a wide variety of therapeutics are under investigation.[7] Some of these low-molecular-weight therapeutics include dexamethasone, methylprednisolone, 17-b-estradiol, angiopeptin, paclitaxel, actinomycin D, sirolimus, and arginine-glycine-aspartic acid (RGD).[8] The last example is particularly interesting, as clinical trials have shown that elution or local delivery of RGD decreased neointimal hyperplasia through the recruitment of circulating endothelial progenitor cells to the site of implantation and promoted arterial re-endothelialization. [8h, 9] Building upon these observations, we designed a peptide-based coating that consists of three distinct peptide domains: an implant-adsorptive sequence, an enzymatically cleavable recognition site, and a therapeutic to be delivered (i.e., RGD). Medical devices such as stents coated w...

show abstract

Endothelialization of Titanium Surfaces

Cited by 44 publications

References 41 publications

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

Aqueous Peptide–TiO₂ Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

Enzymatic Release of a Surface‐Adsorbed RGD Therapeutic from a Cleavable Peptide Anchor

Contact Info

Product

Resources

About

Endothelialization of Titanium Surfaces

Cited by 44 publications

References 41 publications

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

Aqueous Peptide–TiO2 Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

Enzymatic Release of a Surface‐Adsorbed RGD Therapeutic from a Cleavable Peptide Anchor

Contact Info

Product

Resources

About

Aqueous Peptide–TiO₂ Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms