2001
DOI: 10.1016/s0168-3659(01)00262-0
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The coiled coils in the design of protein-based constructs: hybrid hydrogels and epitope displays

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Cited by 53 publications
(42 citation statements)
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“…The coiled coil is one of the basic folding patterns of native proteins, consisting of two or more right-handed amphiphilic α-helices wound together noncovalently to form a slightly left-handed superhelix ( Figure 15) [176][177][178]. The coiled coil domain is based on a heptad repeat unit abcdefg, where a and d are typically hydrophobic amino acids (leucine), and e and g are charged (glutamic acid) [179].…”
Section: Coiled Coil Domainsmentioning
confidence: 99%
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“…The coiled coil is one of the basic folding patterns of native proteins, consisting of two or more right-handed amphiphilic α-helices wound together noncovalently to form a slightly left-handed superhelix ( Figure 15) [176][177][178]. The coiled coil domain is based on a heptad repeat unit abcdefg, where a and d are typically hydrophobic amino acids (leucine), and e and g are charged (glutamic acid) [179].…”
Section: Coiled Coil Domainsmentioning
confidence: 99%
“…This behavior has been exploited to create pH-sensitive and temperature-sensitive hydrogels [176,181]. These genetically encoded hydrogels demonstrated tunable diffusion, which is controlled by the residues composing the heptad sequence as well as the state of the hydrogel (soluble versus collapsed) [178,181].…”
Section: Coiled Coil Domainsmentioning
confidence: 99%
“…Peptidebased materials have also been shown to form hydrogel networks in response to physical or chemical stimuli. [13][14][15][16][17] These materials utilize the primary modes of self-association in peptides, the hydrophobic aggregation of -strands and coiling of helices, to form long-range networks that lead to hydrogel formation. In this work, we have developed new synthetic block copolymers that respond to both pH and temperature, providing the ability to tune the nanoscale and macroscale structures formed using two independent environmental stimuli, giving rise to unique phase behavior and formation of dehydrated elastic solids by self-assembly that has not been seen in other systems.…”
Section: Introductionmentioning
confidence: 99%
“…The architecture of such proteins emulates those of naturally occurring protein multimeric structures, mostly based on a class of protein motifs called coiled-coil motifs. Kopecek et al have synthesized hybrid hydrogel systems using coiled-coil domains to drive the self-assembly of polymer chains [81][82][83]. Coiled-coil induced self-assembly has been shown to be strongly dependent on environmental stimuli such as concentration, temperature, pH, and properties of the solvent.…”
Section: Artificial Protein Hydrogelsmentioning
confidence: 99%
“…Specifically, the designed epitope-display model system consisted of two main components: epitope-containing histidine-tagged peptide, and a synthetic polymer with two types of functionalities, one for covalent attachment to the substrate and the other for peptide immobilization [82].…”
Section: Artificial Protein Hydrogelsmentioning
confidence: 99%