Synthetic lipidation of peptides and amino acids: monolayer structure and properties.

Berndt, Peter; Fields, Gregg B.; Tirrell, Matthew

doi:10.1021/ja00142a019

Cited by 283 publications

(263 citation statements)

References 2 publications

Supporting

Mentioning

262

Contrasting

Order By: Relevance

“…To emulate the triple helical structure of collagen, peptide-amphiphiles (PAs) have been synthesized by Fields, Tirrell and coworkers [66][67][68]. A PA consists of a collagen sequence Gly-Val-Lys-Gly-Asp-Lys-Gly-Asn-Pro-Gly-Trp-Pro-Gly-Ala-Pro connected to a long-chain mono-or di-alkyl ester lipid.…”

Section: Self-assemblymentioning

confidence: 99%

Biomimetic materials for tissue engineering

Peter

2008

Advanced Drug Delivery Reviews

1,185

819

View full text Add to dashboard Cite

Tissue engineering and regenerative medicine is an exciting research area that aims at regenerative alternatives to harvested tissues for transplantation. Biomaterials play a pivotal role as scaffolds to provide three-dimensional templates and synthetic extracellular-matrix environments for tissue regeneration. It is often beneficial for the scaffolds to mimic certain advantageous characteristics of the natural extracellular matrix, or developmental or would healing programs. This article reviews current biomimetic materials approaches in tissue engineering. These include synthesis to achieve certain compositions or properties similar to those of the extracellular matrix, novel processing technologies to achieve structural features mimicking the extracellular matrix on various levels, approaches to emulate cell-extracellular matrix interactions, and biologic delivery strategies to recapitulate a signaling cascade or developmental/would-healing program. The article also provides examples of enhanced cellular/tissue functions and regenerative outcomes, demonstrating the excitement and significance of the biomimetic materials for tissue engineering and regeneration.

show abstract

Section: Self-assemblymentioning

confidence: 99%

Biomimetic materials for tissue engineering

Peter

2008

Advanced Drug Delivery Reviews

1,185

819

View full text Add to dashboard Cite

show abstract

“…High-pressure liquid chromatography with mass spectrometry controlled fraction collection (LCMS; Shimadzu Corp.) utilizing a reversed-phase C8 column (Waters) with a gradient of acetonitrile in Milli-Q water containing 0.1% formic acid was employed to purify J8 peptide. For J8 peptide amphiphiles, the hydrophobic moiety dipalmitoylglutamic acid (diC 16 ) was synthesized by a previously established method (34). J8 peptide was synthesized similarly to above except the C-terminal lysine was protected with DDE instead of Boc which was used for the other lysines.…”

Section: Peptide and Peptide Amphiphile Synthesismentioning

confidence: 99%

Peptide Amphiphile Micelles Self-Adjuvant Group A Streptococcal Vaccination

Trent

Ulery

Black

et al. 2014

AAPS J

View full text Add to dashboard Cite

Abstract. Delivery system design and adjuvant development are crucially important areas of research for improving vaccines. Peptide amphiphile micelles are a class of biomaterials that have the unique potential to function as both vaccine delivery vehicles and self-adjuvants. In this study, peptide amphiphiles comprised of a group A streptococcus B cell antigen (J8) and a dialkyl hydrophobic moiety (diC 16 ) were synthesized and organized into self-assembled micelles, driven by hydrophobic interactions among the alkyl tails. J8-diC 16 formed cylindrical micelles with highly α-helical peptide presented on their surfaces. Both the micelle length and secondary structure were shown to be enhanced by annealing. When injected into mice, J8-diC 16 micelles induced a strong IgG1 antibody response that was comparable to soluble J8 peptide supplemented with two classical adjuvants. It was discovered that micelle adjuvanticity requires the antigen be a part of the micelle since separation of J8 and the micelle was insufficient to induce an immune response. Additionally, the diC 16 tail appears to be non-immunogenic since it does not stimulate a pathogen recognition receptor whose agonist (Pam 3 Cys) possesses a very similar chemical structure. The research presented in this paper demonstrates the promise peptide amphiphile micelles have in improving the field of vaccine engineering.

show abstract

“…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.

1,160

950

View full text Add to dashboard Cite

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...

show abstract

Synthetic lipidation of peptides and amino acids: monolayer structure and properties.

Cited by 283 publications

References 2 publications

Biomimetic materials for tissue engineering

Biomimetic materials for tissue engineering

Peptide Amphiphile Micelles Self-Adjuvant Group A Streptococcal Vaccination

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

Contact Info

Product

Resources

About