2002
DOI: 10.1016/s0142-9612(01)00099-0
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Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence

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Cited by 256 publications
(262 citation statements)
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“…This approach would obviate the need for biotin-streptavidin complexes because the protein could be covalently linked to the peptide. However, it is possible that entropy or steric effects could limit fibril growth (24) and by implication, incorporation of fusion proteins into selfassembling peptide fibrils. In addition, the biotin sandwich approach can be considered a modular building-block strategy that could be used to multifunctionalize an injectable microenvironment.…”
Section: Discussionmentioning
confidence: 99%
“…This approach would obviate the need for biotin-streptavidin complexes because the protein could be covalently linked to the peptide. However, it is possible that entropy or steric effects could limit fibril growth (24) and by implication, incorporation of fusion proteins into selfassembling peptide fibrils. In addition, the biotin sandwich approach can be considered a modular building-block strategy that could be used to multifunctionalize an injectable microenvironment.…”
Section: Discussionmentioning
confidence: 99%
“…Zhang et al have synthesized short oligopeptides having 12 to 16 amino acids that spontaneously form stable β-sheet structures under physiological solution conditions [220][221][222][223][224][225][226][227][228][229][230][231][232][233][234][235]. As shown in Figure 19a, these ionic selfcomplementary oligopeptides have amphiphilic character; one face of the molecule consists of nonpolar, hydrophobic amino acids (such as Ala, Phe, or Leu), and the other face consists of alternating oppositely charged amino acids (such as positively charged Lys or Arg and negatively charged Asp or Glu).…”
Section: β-Sheet Forming Ionic Oligopeptidesmentioning
confidence: 99%
“…4, 23, 24, 25, 26, 27, 28, 29 β ‐sheet peptides are of particular interest as they allow the fabrication of very stable hydrogels with properties that can be tailored through peptide design, media properties and processing. We have recently investigated the self‐assembly and gelation properties of a family of β ‐sheet peptides 30, 31, 32, 33, 34 based on the design developed by Zhang and co‐workers.…”
Section: Introductionmentioning
confidence: 99%