Cellular recognition of synthetic peptide amphiphiles in self-assembled monolayer films

Pakalns, Teika; Haverstick, Kraig; Fields, Gregg B.; McCarthy, James B.; Mooradian, Daniel L.; Tirrell, Matthew

doi:10.1016/s0142-9612(99)00157-x

Cited by 131 publications

(109 citation statements)

References 42 publications

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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.

1,178

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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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.

1,178

950

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“…They also prepared a conjugate which contained loops connected by linkers to dialkyl chains on both sides. 57 It was found that lipid chain attachment to the RGD peptides effected melanoma spreading. The amino conjugated PA was found to hinder spreading, whilst the looped PA was found to promoyr concentrationdependent spreading, and indiscriminate spreading was observed for the carboxyl coupled PA. Further studies based on liposomes revealed that spontaneous metastasis could be inhibited by RGD based PAs.…”

Section: -56mentioning

confidence: 99%

Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials

2017

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Molecular self-assembly is a multi-disciplinary field of research, with potential chemical and biological applications. One of the main driving forces of self-assembly is molecular amphiphilicity, which can drive formation of complex and stable nanostructures. Self-assembling peptide and peptide conjugates have attracted great attention due to their biocompatibility, biodegradability and biofunctionality. Understanding assembly enables the better design of peptide amphiphiles which may form useful and functional nanostructures. This review covers self-assembly of amphiphilic peptides and peptide mimetic materials, as well as their potential applications. Peptide self-assemblySelf-assembly is defined as the ability of a molecule, without guidance of external factors, to associate through non-covalent interactions to form highly ordered 3-dimensional structures.

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“…These LB films can be deposited on polymer surfaces by chemically treating the polymer to attract the LB film and introducing the polymer to a Langmuir-Blodgett trough, allowing a monolayer to form prior to endothelial cell exposure [95].…”

Section: Surface Coatings and Filmsmentioning

confidence: 99%

A Survey of Surface Modification Techniques for Next-Generation Shape Memory Polymer Stent Devices

Govindarajan

Shandas

2014

Polymers

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Abstract:The search for a single material with ideal surface properties and necessary mechanical properties is on-going, especially with regard to cardiovascular stent materials. Since the majority of stent problems arise from surface issues rather than bulk material deficiencies, surface optimization of a material that already contains the necessary bulk properties is an active area of research. Polymers can be surface-modified using a variety of methods to increase hemocompatibilty by reducing either late-stage restenosis or acute thrombogenicity, or both. These modification methods can be extended to shape memory polymers (SMPs), in an effort to make these materials more surface compatible, based on the application. This review focuses on the role of surface modification of materials, mainly polymers, to improve the hemocompatibility of stent materials; additional discussion of other materials commonly used in stents is also provided. Although shape memory polymers are not yet extensively used for stents, they offer numerous benefits that may make them good candidates for next-generation stents. Surface modification techniques discussed here include roughening, patterning, chemical modification, and surface modification for biomolecule and drug delivery.

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Cellular recognition of synthetic peptide amphiphiles in self-assembled monolayer films

Cited by 131 publications

References 42 publications

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

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

Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials

A Survey of Surface Modification Techniques for Next-Generation Shape Memory Polymer Stent Devices

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