Peptide/Protein Hybrid Materials: Enhanced Control of Structure and Improved Performance through Conjugation of Biological and Synthetic Polymers

Vandermeulen, Guido W. M.; Klok, Harm‐Anton

doi:10.1002/mabi.200300079

Cited by 244 publications

(245 citation statements)

References 115 publications

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“…Our work provides a concerted approach to identifying simple smart responses and provides a foundation for future, more elaborate mechanisms to impart smart behavior. This work is a prelude to future protein design and nanoengineering studies, in which peptide polymer scaffolds can be used for the attachment of chemical groups to the peptides that will confer functionality to the structure of the polymer (29).…”

Section: Resultsmentioning

confidence: 99%

Toward the development of peptide nanofilaments and nanoropes as smart materials

Wagner

Phillips

Ali

et al. 2005

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

119

117

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Protein design studies using coiled coils have illustrated the potential of engineering simple peptides to self-associate into polymers and networks. Although basic aspects of self-assembly in protein systems have been demonstrated, it remains a major challenge to create materials whose large-scale structures are well determined from design of local protein-protein interactions. Here, we show the design and characterization of a helical peptide, which uses phased hydrophobic interactions to drive assembly into nanofilaments and fibrils (''nanoropes''). Using the hydrophobic effect to drive self-assembly circumvents problems of uncontrolled self-assembly seen in previous approaches that used electrostatics as a mode for self-assembly. The nanostructures designed here are characterized by biophysical methods including analytical ultracentrifugation, dynamic light scattering, and circular dichroism to measure their solution properties, and atomic force microscopy to study their behavior on surfaces. Additionally, the assembly of such structures can be predictably regulated by using various environmental factors, such as pH, salt, other molecular crowding reagents, and specifically designed ''capping'' peptides. This ability to regulate self-assembly is a critical feature in creating smart peptide biomaterials.biomaterial ͉ coiled coil ͉ protein design ͉ circular dichroism ͉ atomic force microscopy D esigned proteins are valuable paradigms for engineering at the nanoscale, offering favorable properties such as atomiclevel precision and tight regulation of self-assembly by using a variety of environmental cues (i.e., pH, ionic strength, temperature) (1-3). As one of the most well studied and naturally abundant structural motifs in proteins, coiled coils are particularly suited to protein design. Their basic sequence feature, the heptad repeat, is a seven-residue pattern (abcdefg) n of nonpolar and polar residues that gives rise to amphipathic ␣-helices. The hydrophobic effect drives the burial of nonpolar residues at the helix-pairing interface and influences geometric details of resulting structures (4). Electrostatic and polar residues at buried or solvent-exposed locations provide additional means to manipulate structural features by stabilization or destabilization (negative design) of key interactions (5-8).Recent attempts to design self-assembling protein networks by using coiled coils have focused on simple systems, such as linear and branched fibrils (9-14), planar assemblies (15), and hydrogels (16-18). Specifically, filament formation has been achieved by stabilization of intermediate structures that foster intermolecular coiled-coil interactions (11)(12)(13)(14). Previous studies have reported the design of short helical peptides, which interact via a dimeric coiled-coil motif and are stabilized by a combination of overlapping hydrophobic and electrostatic intermolecular interactions (9, 13, 14). These peptides do indeed self-assemble into filaments; however, these filaments also show evidence of extensive...

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Section: Resultsmentioning

confidence: 99%

Toward the development of peptide nanofilaments and nanoropes as smart materials

Wagner

Phillips

Ali

et al. 2005

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

119

117

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“…124 Amyloid fibrils of insulin have been shown to possess a large void space able to accommodate molecular iodine. Iodine molecules seem to be solvent accessible and can eventually be released.…”

Section: Amyloid-based Drug Deliverymentioning

confidence: 99%

Amyloid-based nanosensors and nanodevices

2014

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Self-assembling amyloid-like peptides and proteins give rise to promising biomaterials with potential applications in many fields. Amyloid structures are formed by the process of molecular recognition and self-assembly, wherein a peptide or protein monomer spontaneously self-associates into dimers and oligomers and subsequently into supramolecular aggregates, finally resulting in condensed fibrils. Mature amyloid fibrils possess a quasi-crystalline structure featuring a characteristic fiber diffraction pattern and have well-defined properties, in contrast to many amorphous protein aggregates that arise when proteins misfold. Core sequences of four to seven amino acids have been identified within natural amyloid proteins. They are capable to form amyloid fibers and fibrils and have been used as amyloid model structures, simplifying the investigations on amyloid structures due to their small size. Recent studies have highlighted the use of self-assembled amyloid-based fibers as nanomaterials. Here, we discuss the latest advances and the major challenges in developing amyloids for future applications in nanotechnology and nanomedicine, with the focus on development of sensors to study protein-ligand interactions.

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“…By introducing desired interactions such as H-bonds and charge compensation, highly ordered organizations can be created. [37,38] We synthesized Ac-K 6 -gA, a positively charged derivative of Ac-E 6 -gA, then mixed both materials together. In a series of TEM images, it was shown that instead of vesicles, multilamellar structures were generated from a molar ratio of 0.3 to 0.8.…”

Section: Micelles and Fibersmentioning

confidence: 99%

Self-assembled Structures from Amphiphilic Peptides

Sigg¹,

Schuster²,

Meier

2013

Chimia

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Nanotechnology and its applications are strongly influenced by structures self-assembled from a variety of different materials. This review covers nanostructures, including micelles, rod-like micelles, fibers and peptide beads, self-assembled from de novo designed amphiphilic peptides. The latter are promising candidates for the development of nanoscale carrier systems because they are completely composed of amino acids. In addition to designing primary sequences, secondary structure and external parameters are also discussed with respect to their impact on self-assembly. Moreover, the assembly process itself is examined. Potential applications range from gene and drug delivery devices to diagnostics, thereby highlighting the versatility of the system.

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Peptide/Protein Hybrid Materials: Enhanced Control of Structure and Improved Performance through Conjugation of Biological and Synthetic Polymers

Cited by 244 publications

References 115 publications

Toward the development of peptide nanofilaments and nanoropes as smart materials

Toward the development of peptide nanofilaments and nanoropes as smart materials

Amyloid-based nanosensors and nanodevices

Self-assembled Structures from Amphiphilic Peptides

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