Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

Pierschbacher, Michael D.; Ruoslahti, Erkki

doi:10.1038/309030a0

Cited by 3,426 publications

(2,143 citation statements)

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“…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%

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

Sultan

Westcott

Hughes

et al. 2016

ACS Appl. Mater. Interfaces

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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

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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

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“…The Arg-Gly-Asp (RGD) motif was originally identified as the site within fibronectin that mediates cell attachment [1]. Soon thereafter it was demonstrated that several other extracellular proteins containing an RGD motif play a role in cell adhesion processes in many different mammalian tissues via their RGD functional site.…”

Section: Introductionmentioning

confidence: 99%

High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif

Senchou

Weide

Carrasco

et al. 2004

Cellular and Molecular Life Sciences (CMLS)

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“…26 In attempts to address these issues, several laboratories have developed compliant polyurethane composites. [27][28][29] In the approach presented here, we focus on elastin, which forms a crosslinked network in the arterial wall 30 and which, along with collagen, imparts elasticity and resiliency to the M-MASMTGGQQMG-HHHHHHH-DDDDK(LD-YAVTGRGDSPASSKPIA((VPGIG) 2 VPGKG(VPGIG) 2 ) 4 VP) 3 [41][42][43] this sequence serves as a ligand for the α v β 3 and α 5 β 1 integrins. 44,45 aECM 2 is a negative control for aECM 1, in which the sequence of the RGD cellbinding domain has been scrambled.…”

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confidence: 99%

Comparative Cell Response to Artificial Extracellular Matrix Proteins Containing the RGD and CS5 Cell-Binding Domains

2004

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This study addresses endothelial cell adhesion and spreading on a family of artificial extracellular matrix (aECM) proteins designed for application in small-diameter vascular grafts. The aECM proteins contain domains derived from elastin and from fibronectin. aECM 1 contains the RGD sequence from the tenth type III domain of fibronectin; aECM 3 contains the fibronectin CS5 cell-binding domain. Negative control proteins aECM 2 and 4 are scrambled versions of aECM 1 and 3, respectively.Competitive peptide inhibition studies and comparisons of positive and negative control proteins confirm that adhesion of HUVECs to aECM proteins 1 and 3 is sequence specific. When subjected to a normal detachment force of 780 pN, 3-fold more HUVEC remained adherent to aECM 1 than to aECM 3. HUVEC also spread more rapidly on aECM 1 than on aECM 3. These results (i) indicate that cellular responses to aECM proteins can be modulated through choice of cell-binding domain, and (ii) recommend the RGD sequence for applications that require rapid endothelial cell spreading and matrix adhesion. IntroductionCardiovascular disease afflicts more than 61 million Americans 1 and causes 4 million deaths each year in Europe. 2 Severe atherosclerosis often requires surgical removal of the affected tissue and implantation of an autologous or synthetic vascular graft. The most widely used materials in synthetic vascular grafts are poly(ethylene terephthalate) (PET) and expanded poly(tetrafluoroethylene) (ePTFE); when used in small-diameter grafts, both materials are characterized by high failure rates due to thrombosis and intimal hyperplasia. [3][4][5] Autologous saphenous vein yields higher patency rates than synthetic materials, particularly when used to reconstruct the infrapopliteal artery, 6,7 but autologous vein is limited in supply and patients often suffer from coexisting disease that makes these vessels unsuitable as grafts. 5,8 A family of artificial proteins that exhibits some of the essential characteristics of the extracellular matrix has been developed for application in small-diameter vascular grafts. [9][10][11][12][13] Artificial matrices that incorporate functional protein domains have been produced for a variety of applications. [14][15][16][17] The artificial extracellular matrix (aECM) proteins in this study consist of domains derived from elastin and fibronectin ( contains a T7 tag, a heptahistidine tag, an enterokinase cleavage site, and elastin-like domains containing lysine residues for crosslinking. The RGD cell-binding domain is found in aECM 1, whereas the minimal recognition sequence in the RGD cell-binding domain has been scrambled in aECM 2 to provide a negative control. aECM 3 includes the CS5 cell-binding domain whereas aECM 4, the negative control, contains a scrambled version of the CS5 cell-binding domain.An important criterion in the design of aECM proteins is the tensile modulus; compliance mismatch between the graft and tissue has been strongly implicated in graft failure. It is believed that flow...

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Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

Cited by 3,426 publications

References 32 publications

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

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

High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif

Comparative Cell Response to Artificial Extracellular Matrix Proteins Containing the RGD and CS5 Cell-Binding Domains

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Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

Cited by 3,426 publications

References 32 publications

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

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

High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif

Comparative Cell Response to Artificial Extracellular Matrix Proteins Containing the RGD and CS5 Cell-Binding Domains

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

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