Engineered and designed peptide-based fibrous biomaterials
Source abstract
Abstract
Our increasing understanding of peptide and protein folding and assembly raises new possibilities for engineering novel self-assembling supramolecular structures and bio-inspired materials. Here we focus on peptides designed de novo, and natural systems that have been engineered to form extended protein fibres. Potential applications of such assemblies include the preparation of functionalised biomaterials for the development of new diagnostic devices, scaffolds to recruit cells for cell/tissue engineering, and templates for the assembly of inorganic materials.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Supramolecular Self-Assembly in Materials · Chemical Synthesis and Analysis · Polydiacetylene-based materials and applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (74)
Show source-provided references
1. Pollard · 2002
2. 1999
3. Branden · 1999
4. Biomedicine––Toxic proteins in neurodegenerative disease10.1126/science.1067122 ↗
5. Parkinson's disease and related synucleinopathies are a new class of nervous system amyloidoses10.1016/S0161-813X(02)00065-7 ↗
6. Mechanisms of disease: islet amyloid and type 2 diabetes mellitus10.1056/NEJM200008103430607 ↗
7. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders10.1016/S0896-6273(02)00872-3 ↗
8. Huntington's disease: the challenge for cell biologists10.1016/S0962-8924(00)01853-5 ↗
9. Altered aggregation properties of mutant gammacrystallins cause inherited cataract10.1093/emboj/cdf609 ↗
10. Common core structure of amyloid fibrils by synchrotron X-ray diffraction10.1006/jmbi.1997.1348 ↗
11. Cryoelectron microscopy structure of an SH3 amyloid fibril and model of the molecular packing10.1093/emboj/18.4.815 ↗
12. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR10.1073/pnas.262663499 ↗
13. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril10.1073/pnas.252625999 ↗
14. Structure and texture of fibrous crystals formed by Alzheimer's Aβ(11–25) peptide fragment10.1016/S0969-2126(03)00149-7 ↗
15. Protein-misfolding diseases: getting out of shape10.1038/418729a ↗
16. Structural regulation of a peptide-conjugated graft copolymer: a simple model for amyloid formation10.1002/chem.200390132 ↗
17. Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures10.1021/ja0029580 ↗
18. Amyloid architecture: complementary assembly of heterogeneous combinations of three or four peptides into amyloid fibrils10.1002/1439-7633(20020703)3:7<637::AID-CBIC637>3.0.CO;2-9 ↗
19. Hydrophobins, the fungal coat unravelled10.1016/S0304-4157(00)00002-2 ↗
20. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils10.1101/gad.264303 ↗
21. The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor10.1101/gad.264403 ↗
22. How a fungus escapes the water to grow into the air10.1016/S0960-9822(99)80019-0 ↗
23. The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures10.1016/S0969-2126(00)00559-1 ↗
24. Interfacial self-assembly of a fungal hydrophobin into a hydrophobic rodlet layer10.1105/tpc.5.11.1567 ↗
25. Interfacial self-assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces10.1002/j.1460-2075.1994.tb06929.x ↗
26. Role of Escherichia coli curli operons in directing amyloid fiber formation10.1126/science.1067484 ↗
27. The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, pyrococcus furiosus10.1021/bi991406v ↗
28. Freezing of a fish antifreeze protein results in amyloid fibril formation10.1016/S0006-3495(03)74874-7 ↗
29. Survival of water stress in annual fish embryos: dehydration avoidance and egg envelope amyloid fibers
30. Amyloids protect the silkmoth oocyte and embryo10.1016/S0014-5793(00)01888-3 ↗
31. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils, and fibers10.1073/pnas.191250198 ↗
32. Evolution of a strain of CJD that induces BSE-like plaques10.1126/science.277.5322.94 ↗
33. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains10.1110/ps.8.3.509 ↗
34. Hydrogels in pharmaceutical formulations10.1016/S0939-6411(00)00090-4 ↗
35. Functional hydrogel structures for autonomous flow control inside microfluidic channels10.1038/35007047 ↗
36. Hydrogels for tissue engineering10.1021/cr000108x ↗
37. Novel peptide-based biomaterial scaffolds for tissue engineering10.1016/S0167-7799(01)01840-6 ↗
38. Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds10.1073/pnas.97.12.6728 ↗
39. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane10.1073/pnas.90.8.3334 ↗
40. Left-handed helical ribbon intermediates in the self-assembly of a beta-sheet peptide10.1021/nl015697g ↗
41. Design of nanostructured biological materials through self-assembly of peptides and proteins10.1016/S1367-5931(02)00391-5 ↗
42. Self-complementary oligopeptide matrices support mammalian-cell attachment10.1016/0142-9612(95)96874-Y ↗
43. Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair10.1073/pnas.142309999 ↗
44. Self-assembly of a designed protein polymer into beta-sheet fibrils and responsive gels10.1021/ma025952z ↗
45. Reversible hydrogels from self-assembling artificial proteins10.1126/science.281.5375.389 ↗
46. Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles10.1038/417424a ↗
47. Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide10.1021/ja027993g ↗
48. Mutational analysis of designed peptides that undergo structural transition from alpha helix to beta sheet and amyloid fibril formation10.1016/S0969-2126(00)00183-0 ↗
49. Construction of peptides that undergo structural transition from alpha-helix to beta-sheet and amyloid fibril formation by the introduction of N-terminal hydrophobic amino acids10.1016/S0040-4020(00)00524-X ↗
50. Heterogeneous assembly of complementary peptide pairs into amyloid fibrils with alpha–beta structural transition10.1002/1439-7633(20010105)2:1<75::AID-CBIC75>3.0.CO;2-U ↗
51. Conformational behavior of ionic self-complementary peptides10.1110/ps.9.6.1095 ↗
52. A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins10.1074/jbc.M107663200 ↗
53. Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition10.1073/pnas.0431081100 ↗
54. Casting metal nanowires within discrete self-assembled peptide nanotubes10.1126/science.1082387 ↗
55. De novo amyloid proteins from designed combinatorial libraries10.1073/pnas.96.20.11211 ↗
56. Template-directed assembly of a de novo designed protein10.1021/ja0261271 ↗
57. Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science10.1021/ja9937831 ↗
58. Self-assembly of Aβ(10–35)-PEG block copolymer fibrils10.1021/ja991233x ↗
59. First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with non-coded amino acids10.1039/b105418j ↗
60. Fibril-forming model synthetic peptides containing 3-aminophenylacetic acid10.1016/S0040-4020(02)01093-1 ↗
61. Coiled coils: new structures and new functions
62. Coiled coils: a highly versatile protein folding motif10.1016/S0962-8924(00)01898-5 ↗
63. De novo design of alpha-helical coiled coils and bundles: models for the development of protein-design principles10.1016/S0167-7799(98)01212-8 ↗
64. Core-directed protein design10.1016/S0959-440X(00)00234-7 ↗
65. Fibril formation by an amphipathic alpha-helix-forming polypeptide produced by gene engineering10.2183/pjab.73.7 ↗
66. Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis10.1021/bi000246g ↗
67. Design of three-dimensional domain-swapped dimers and fibrous oligomers10.1073/pnas.98.4.1404 ↗
68. De novo design of fibrils made of short alpha-helical coiled coil peptides10.1016/S1074-5521(01)00073-4 ↗
69. Engineering the morphology of a selfassembling protein fibre10.1038/nmat885 ↗
70. Introducing branches into a self-assembling peptide fiber10.1002/anie.200351418 ↗
71. Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments10.1073/pnas.041614998 ↗
72. Designing supramolecular protein assemblies10.1016/S0959-440X(02)00350-0 ↗
73. Design of protein struts for self-assembling nanoconstructs10.1073/pnas.132544299 ↗
74. S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays10.1073/pnas.232299399 ↗