Self-assembling Behavior of Designer Lipid-like Peptides
TL;DR: A class of lipid-like peptides that are less than 10 natural amino acids in length and structurally amphiphilic exhibit self-assembling behavior akin to some lipids, with distinct critical aggregate concentration values and sequestration of the hydrophobic tails away from water.
Abstract: Even though enormous progress has been made in our understanding of soluble proteins and enzymes, our knowledge of membrane proteins, particularly integral membrane proteins, still lags far behind. Although a large number of chemical detergents and lipids are available, so far they are inadequate for tackling the problem of solubilizing and stabilizing membrane proteins outside of the lipid bilayer. Thus, the development of new detergents and lipid-like molecules is an important prerequisite for solving those problems. We have designed a class of lipid-like peptides that are less than 10 natural amino acids in length and structurally amphiphilic. Each peptide consists of a hydrophilic head-group composed of charged or polar residues and a hydrophobic tail consisting of a string of hydrophobic amino acids. In aqueous solutions, they self-organize to form different supramolecular structures such as vesicles, nanotubes or membranes. It has been shown that they stabilize the functions of several membrane prot...
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TL;DR: This critical review highlights recent advances in studying peptide amphiphiles, focusing on the formation of different nanostructures and their applications in diverse fields.
Abstract: Short synthetic peptide amphiphiles have recently been explored as effective nanobiomaterials in applications ranging from controlled gene and drug release, skin care, nanofabrication, biomineralization, membrane protein stabilization to 3D cell culture and tissue engineering. This range of applications is heavily linked to their unique nanostructures, remarkable simplicity and biocompatibility. Some peptide amphiphiles also possess antimicrobial activities whilst remaining benign to mammalian cells. These attractive features are inherently related to their selective affinity to different membrane interfaces, high capacity for interfacial adsorption, nanostructuring and spontaneous formation of nano-assemblies. Apart from sizes, the primary sequences of short peptides are very diverse as they can be either biomimetic or de novo designed. Thus, their self-assembling mechanistic processes and the nanostructures also vary enormously. This critical review highlights recent advances in studying peptide amphiphiles, focusing on the formation of different nanostructures and their applications in diverse fields. Many interesting features learned from peptide self-organisation and hierarchical templating will serve as useful guidance for functional materials design and nanobiotechnology (123 references).
573 citations
TL;DR: Molecular design of new materials using short peptides is poised to become increasingly important in biomedical research, biomedical technology and medicine, and is covered in this tutorial review.
Abstract: Scientists and bioengineers have dreamed of designing materials from the bottom up with the finest detail and ultimate control at the single molecular level. The discovery of a class of self-assembling peptides that spontaneously undergo self-organization into well-ordered structures opened a new avenue for molecular fabrication of biological materials. Since this discovery, diverse classes of short peptides have been invented with broad applications, including 3D tissue cell culture, reparative and regenerative medicine, tissue engineering, slow drug release and medical device development. Molecular design of new materials using short peptides is poised to become increasingly important in biomedical research, biomedical technology and medicine, and is covered in this tutorial review.
317 citations
TL;DR: The self‐assembly of several classes of amphiphilic peptides is reviewed, and selected applications are discussed, and the influence of environmental variables such as pH and temperature on aggregate nanostructure is discussed.
Abstract: The self-assembly of several classes of amphiphilic peptides is reviewed, and selected applications are discussed. We discuss recent work on the self-assembly of lipopeptides, surfactant-like peptides and amyloid peptides derived from the amyloid-β peptide. The influence of environmental variables such as pH and temperature on aggregate nanostructure is discussed. Enzyme-induced remodelling due to peptide cleavage and nanostructure control through photocleavage or photo-cross-linking are also considered. Lastly, selected applications of amphiphilic peptides in biomedicine and materials science are outlined. © 2014 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons, Ltd.
282 citations
TL;DR: This tutorial review focuses on two self-assembling peptide systems that can be designed for new materials and nanodevices from the bottom up.
Abstract: Chemistry has generally been associated with inorganic and organic syntheses, metal-organic composites, coordinate metal chemistry, catalyses, block copolymer, coating, thin film, industrial surfactants and small-molecule drug development. That is about to change. Chemistry will also expand to the discovery and fabrication of biological and molecular materials with diverse structures, functionalities and utilities. The advent of biotechnology, nanotechnology and nanobiotechnology has accelerated this trend. Nature has selected and evolved numerous molecular architectural motifs at nanometer scale over billions of years for particular functions. These molecular nanomotifs can now be designed for new materials and nanodevices from the bottom up. Chemistry will again harness Nature's enormous power to benefit other disciplines and society. This tutorial review focuses on two self-assembling peptide systems.
256 citations
TL;DR: The field of chiral self-assembling peptide nanobiotechnology is growing in a number of directions that has led to many surprises in areas of novel materials, synthetic biology, clinical medicine and beyond.
Abstract: Chirality is absolutely central in chemistry and biology. The recent findings of chiral self-assembling peptides’ remarkable chemical complementarity and structural compatibility make it one of the most inspired designer materials and structures in nanobiotechnology. The emerging field of designer chemistry and biology further explores biological and medical applications of these simple D,L- amino acids through producing marvellous nanostructures under physiological conditions. These self-assembled structures include well-ordered nanofibers, nanotubes and nanovesicles. These structures have been used for 3-dimensional tissue cultures of primary cells and stem cells, sustained release of small molecules, growth factors and monoclonal antibodies, accelerated wound-healing in reparative and regenerative medicine as well as tissue engineering. Recent advances in molecular designs have also led to the development of 3D fine-tuned bioactive tissue culture scaffolds. They are also used to stabilize membrane proteins including difficult G-protein coupled receptors for designing nanobiodevices. One of the self-assembling peptides has been used in human clinical trials for accelerated wound-healings. It is our hope that these peptide materials will open doors for more and diverse clinical uses. The field of chiral self-assembling peptide nanobiotechnology is growing in a number of directions that has led to many surprises in areas of novel materials, synthetic biology, clinical medicine and beyond.
189 citations
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TL;DR: In this paper, a simple theory is developed that accounts for many of the observed physical properties of micelles, both globular and rod-like, and of bilayer vesicles composed of ionic or zwitterionic amphiphiles.
Abstract: A simple theory is developed that accounts for many of the observed physical properties of micelles, both globular and rod-like, and of bilayer vesicles composed of ionic or zwitterionic amphiphiles. The main point of departure from previous theories lies in the recognition and elucidation of the role of geometric constraints in self-assembly. The linking together of thermodynamics, interaction free energies and geometry results in a general framework which permits extension to more complicated self-assembly problems.
4,563 citations
TL;DR: In this article, it was shown that in the presence of polar solvents, there is a significant enhancement in the intensity of the 0-0 vibronic band at the expense of other bands.
Abstract: The fluorescence intensities for various vibronic fine structures in the pyrene monomer fluorescence show strong solvent dependence. In the presence of polar solvents, there is a significant enhancement in the intensity of the 0--0 vibronic band at the expense of other bands. This strong perturbation in the vibronic band intensities is more dependent on the solvent dipole moment than on the bulk solvent dielectric constant. This suggests the operation of some specific solute--solvent dipole--dipole interaction mechanism. The strong perturbation of the vibronic band intensities has been used as a probe to accurately determine critical micelle concentrations and also to investigate the extent of water penetration in micellar systems.
3,271 citations
TL;DR: Detailed statistical analyses of integral membrane proteins of the helix‐bundle class from eubacterial, archaean, and eukaryotic organisms for which genome‐wide sequence data are available suggest that uni‐cellular organisms appear to prefer proteins with 6 and 12 transmembrane segments, whereas Caenorhabditis elegans and Homo sapiens have a slight preference for proteins with seven transmemBRane segments.
Abstract: We have carried out detailed statistical analyses of integral membrane proteins of the helix-bundle class from eubacterial, archaean, and eukaryotic organisms for which genome-wide sequence data are available. Twenty to 30% of all ORFs are predicted to encode membrane proteins, with the larger genomes containing a higher fraction than the smaller ones. Although there is a general tendency that proteins with a smaller number of transmembrane segments are more prevalent than those with many, uni-cellular organisms appear to prefer proteins with 6 and 12 transmembrane segments, whereas Caenorhabditis elegans and Homo sapiens have a slight preference for proteins with seven transmembrane segments. In all organisms, there is a tendency that membrane proteins either have many transmembrane segments with short connecting loops or few transmembrane segments with large extra-membraneous domains. Membrane proteins from all organisms studied, except possibly the archaeon Methanococcus jannaschii, follow the so-called "positive-inside" rule; i.e., they tend to have a higher frequency of positively charged residues in cytoplasmic than in extra-cytoplasmic segments.
1,519 citations
Book•
01 Mar 2013
TL;DR: The goal of this series is to pinpoint areas of chemistry where recent progress has outpaced what is covered in any available textbooks, and then seek out and persuade experts in these fields to produce relatively concise but instructive introductions to their fields.
Abstract: New textbooks at all levels of chemistry appear with great regularity. Some fields like basic biochemistry, organic reaction mechanisms, and chemical thermody namics are well represented by many excellent texts, and new or revised editions are published sufficiently often to keep up with progress in research. However, some areas of chemistry, especially many of those taught at the graduate level, suffer from a real lack of up-to-date textbooks. The most serious needs occur in fields that are rapidly changing. Textbooks in these subjects usually have to be written by scientists actually involved in the research which is advancing the field. It is not often easy to persuade such individuals to set time aside to help spread the knowledge they have accumulated. Our goal, in this series, is to pinpoint areas of chemistry where recent progress has outpaced what is covered in any available textbooks, and then seek out and persuade experts in these fields to produce relatively concise but instructive introductions to their fields. These should serve the needs of one semester or one quarter graduate courses in chemistry and biochemistry. In some cases, the availability of texts in active research areas should help stimulate the creation of new courses."
1,446 citations
TL;DR: The nature of detergent binding by the membrane from a noncooperative to a cooperative interaction already below the critical micellar concentration is considered and it is concluded that in general binding as a monolayer ring, rather than as a micelle, is the most probable mechanism.
985 citations