[26] Construction of biologically active protein molecular architecture using self-assembling peptide-amphiphiles

Yu, Ying Ching; Pakalns, Teika; Dori, Yoav; McCarthy, James B.; Tirrell, Matthew; Fields, Gregg B.

doi:10.1016/s0076-6879(97)89065-9

Cited by 63 publications

(90 citation statements)

References 64 publications

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“…The transfer of peptide-amphiphiles to hydrophobic surfaces and the subsequent effect of the surface on peptide conformation and orientation have been studied extensively. Atomic force microscopy shows the appropriate height "differential" for peptide-amphiphiles and lipids if peptide-amphiphiles are oriented upright (34,36). Neutron reflectivity data for triple helical peptideamphiphiles demonstrated that peptide head groups are oriented perpendicular to the air-water interface and retain the same conformation as in solution (36,45).…”

Section: Discussionmentioning

confidence: 99%

Induction of Endothelial Cell Activation by a Triple Helical α2β1 Integrin Ligand, Derived from Type I Collagen α1(I)496–507

Baronas-Lowell

Lauer‐Fields

Fields

2004

Journal of Biological Chemistry

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Endothelial cell activation involves the elevated expression of cell adhesion molecules, chemoattractants, chemokines, and cytokines. These expression profiles may be regulated by integrin-mediated cell signaling pathways. In the current study, an ␣ 2 ␤ 1 integrin triple helical peptide ligand derived from type I collagen residues ␣1(I)496 -507 was examined for induction of human aortic endothelial cell (HAEC) activation. In addition, a "miniextracellular matrix" composed of a mixture of the ␣1(I)496 -507 ligand and a second, ␣-helical ligand incorporating the endothelial cell proliferating region of SPARC (secreted protein acidic and rich in cysteine) was studied for induction of HAEC activation. Following HAEC adhesion to ␣1(I)496 -507, mRNA expression of Eselectin-1, vascular and intercellular cell adhesion molecules-1, and monocytic chemoattractant protein-1 was stimulated, whereas that of endothelin-1 was inhibited. Enzyme-linked immunosorbent assay analysis demonstrated that E-selectin-1 and monocytic chemoattractant protein-1 expression was also stimulated, whereas endothelin-1 protein expression diminished. Engagement of the ␣ 2 ␤ 1 integrin initiated a HAEC response similar to that of tumor necrosis factor-␣-induced HAECs but was not sufficient to induce an inflammatory response. Addition of the SPARC 119 -122 region had only a slight effect on HAEC activation. Other cell-extracellular matrix interactions appear to be required to elicit an inflammatory response. The ␣ 2 ␤ 1 integrin specific triple helical peptide ligand described herein represents a more general in vitro model system by which gene expression and protein production profiles induced by binding to a single cellular receptor type can be quantified.Blood vessels are lined with a contiguous endothelial cell layer. The endothelium lies just inside the medial cell layer of vascular smooth muscle cells, which, in turn, is surrounded by a layer of connective tissue. The location of the endothelial cell lining is such that it provides the interface between the flowing blood and the medial layer of the vessel.The endothelium, under normal physiological conditions, does not bind elements in the flowing blood but instead associates with smooth muscle cells and the extracellular matrix (ECM).1 These normal cell-cell and cell-matrix interactions are maintained, in part, by integrins on the endothelial cell surface (for review, see Ref. 1). Many integrins are involved in cellmatrix interactions; for example, five integrins

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Section: Discussionmentioning

confidence: 99%

Induction of Endothelial Cell Activation by a Triple Helical α2β1 Integrin Ligand, Derived from Type I Collagen α1(I)496–507

Baronas-Lowell

Lauer‐Fields

Fields

2004

Journal of Biological Chemistry

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“…Prior work has shown that construction of peptide-amphiphiles, whereby an alkyl chain is incorporated onto the N terminus of a peptide, results in enhanced thermal stability of peptide conformation and improved binding to hydrophobic surfaces (3,14,18,19,57). The melting temperatures of the peptide-amphiphiles were 45.0 and 48.5°C for C 16 -(Gly-Pro-Hyp) 4 -IV-H1-(Gly-Pro-Hyp) 4 -NH 2 and C 16 -Hyl(Gal) 1265 -(Gly-Pro-Hyp) 4 -IV-H1-(Gly-Pro-Hyp) 4 -NH 2 , respectively (Table I).…”

Section: Construction and Characterization Of Ligandsmentioning

confidence: 99%

“…In addition to the integrin binding sites, the ␣1(IV)1263-1277 region from type IV collagen (gene-derived sequence GlyVal-Lys-Gly-Asp-Lys-Gly-Asn-Pro-Gly-Trp-Pro-Gly-Ala-Pro, designated IV-H1), promotes melanoma cell adhesion, spreading, and signaling (1,3,(12)(13)(14). Affinity chromatography studies with a single-stranded IV-H1 peptide resulted in the isolation of melanoma cell CD44 receptors, in the chondroitin sulfate proteoglycan (CSPG) form (15,16).…”

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confidence: 99%

Melanoma Cell CD44 Interaction with the α1(IV)1263–1277 Region from Basement Membrane Collagen Is Modulated by Ligand Glycosylation

Lauer‐Fields¹,

Malkar²,

Richet³

et al. 2003

Journal of Biological Chemistry

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Tumor cell invasion, a key step in the metastatic process, involves a complex series of correlated macromolecular interactions. These include interaction with, and movement through, collagen, most often type I and/or basement membrane (type IV) collagen. In general, invasion of the basement membrane is believed to be a critical step in the metastatic process. Human melanoma cells have been shown to bind distinct triple-helical regions within type IV collagen (1-5). Melanoma receptors for triple-helical collagen fall into one of two categories: members of the integrin heterodimeric protein family (␣ 1 ␤ 1 , ␣ 2 ␤ 1 , and ␣ 3 ␤ 1 integrins) or cell surface proteoglycans (such as CD44 and melanoma-associated proteoglycan/melanoma chondroitin sulfate proteoglycan (MPG/MCSP/NG2)).

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“…Depending on the composition, amphiphilic peptides have been shown to organize peptide secondary structure and aggregation state (27)(28)(29)(30). PAs synthesized previously with mono-or di-alkyl tails were found to associate in conformations such as triple helical structures found in collagen (31)(32)(33)(34)(35)(36)(37)(38). Modification of this strategy allowed us to design a cone-shaped, ionic amphiphile that could assemble into cylindrical micelles or peptide nanofibers (17).…”

mentioning

confidence: 99%

Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials

Hartgerink

Beniash

Stupp

2002

Proc. Natl. Acad. Sci. U.S.A.

1,170

950

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Twelve derivatives of peptide-amphiphile molecules, designed to self-assemble into nanofibers, are described. The scope of amino acid selection and alkyl tail modification in the peptide-amphiphile molecules are investigated, yielding nanofibers varying in morphology, surface chemistry, and potential bioactivity. The results demonstrate the chemically versatile nature of this supramolecular system and its high potential for manufacturing nanomaterials. In addition, three different modes of self-assembly resulting in nanofibers are described, including pH control, divalent ion induction, and concentration. P reprogrammed noncovalent bonds, within and between molecules, build highly functional and dynamic structures in biology, which motivates our interest in self-assembly of synthetic systems. Over the past few decades a substantial amount of literature describing noncovalent self-assembly of nanostructures has accumulated (1-14). However, it is still difficult to design supramolecular structures, particularly if we want to start with designed molecules and form objects that measure between nanoscopic and macroscopic dimensions. Developing this ability will take us closer to the broad, bottom-up approach of selfassembly observed in biology.Our laboratory has studied over the past decade self-assembly of designed molecules into macromolecular structures of twodimensional (15, 16), one-dimensional (17, 18), and zerodimensional nature (19)(20)(21)(22). These self-assembled objects contain between 10 1 and 10 5 molecules and thus resemble synthetic and biological polymers in molar mass. The interactions that lead to the formation of these structures include chiral dipole-dipole interactions, -stacking, hydrogen bonds, nonspecific van der Waals interactions, hydrophobic forces, electrostatic interactions, and repulsive steric forces. All systems studied involved combinations of these forces that counterbalance the enormous translational and rotational entropic cost caused by polymolecular aggregation. In some cases the possibility of internally linking these self-assembled structures through covalent bonds has been explored (1,17,20,23). A cross-linking produces actual polymers whose various shapes and dimensionalities are controlled by self-assembly and are very different from the well-known ''beads-on-a-chain'' structures of traditional polymers.In our studies of self-assembling systems we also have explored self-organization at length scales much greater than those of the aggregates themselves, reaching into scales of microns, millimeters, and even centimeters. We also have been interested in functionalities that emerge from self-assembly at these largerlength scales. An interesting example was the layering and polar stacking of mushroom-shaped supramolecular structures each measuring about 5 nm. The stem-to-cap layers of these nanostructures result in centimeter-scale films that are spontaneously piezoelectric (24). The search for useful systems in the microscopic and macroscopic regime that take advantage of mole...

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[26] Construction of biologically active protein molecular architecture using self-assembling peptide-amphiphiles

Cited by 63 publications

References 64 publications

Induction of Endothelial Cell Activation by a Triple Helical α2β1 Integrin Ligand, Derived from Type I Collagen α1(I)496–507

Induction of Endothelial Cell Activation by a Triple Helical α2β1 Integrin Ligand, Derived from Type I Collagen α1(I)496–507

Melanoma Cell CD44 Interaction with the α1(IV)1263–1277 Region from Basement Membrane Collagen Is Modulated by Ligand Glycosylation

Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials

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