Citation: Ying Li, Yi Cao. The Physical Chemistry for the Self-assembly of Peptide Hydrogels[J]. Chinese Journal of Polymer Science, ;2018, 36(3): 366-378. doi: 10.1007/s10118-018-2099-6 shu

The Physical Chemistry for the Self-assembly of Peptide Hydrogels

Ying Li ^a ,
Yi Cao ^b,,

a.
Collaborative Innovation Center of Atmospheric Environment and Equipment Technology, School of Environmental Science and Engineering, Jiangsu Engineering Technology Research Centre of Environmental Cleaning Materials, Jiangsu Key Laboratory of Atmospheric Environment Monitoring and Pollution Control, Jiangsu Joint Laboratory of Atmospheric Pollution Control, Nanjing University of Information Science & Technology, Nanjing 210044, China
b.
Collaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing 210093, China

Corresponding author: Yi Cao, caoyi@nju.edu.cn
Received Date: 3 November 2017
Accepted Date: 3 December 2017
Available Online: 28 December 2017

Peptide hydrogels have been widely used for diverse biomedical applications. However, our current understanding of the physical principles underlying the self-assembly process is still limited. In this review, we summarize our current understanding on the physical chemistry principles from the basic interactions that drive the self-assembly process to the energy landscapes that dictate the thermodynamics and kinetics of the process. We discuss the effect of different factors that affect the kinetics of the self-assembly of peptide fibrils and how this is related to the macroscopic gelation process. We provide our understanding on the molecular origin of the complex and rugged energy landscape for the self-assembly of peptide hydrogels. The hierarchical self-assembled structures and the diverse self-assembling mechanism make it difficult and challenging to rationally design the physical and chemical properties of peptide hydrogels at the molecular level. We also give our personal perspective to the potential future directions in this field.
- Hydrogel,
- Peptide,
- Self-assembly,
- Kinetics,
- Thermodynamics
1. [1]
  Lehn J. M.. Perspectives in supramolecular chemistry-from molecular recognition towards molecular informationprocessing and self-organization[J]. Angew. Chem. Int. Ed., 1990,29(11):1304-1319. doi: 10.1002/(ISSN)1521-3773
2. [2]
  Whitesides G. M., Mathias J. P., Seto C. T.. Molecular self-assembly and nanochemistry-a chemical strategy for the synthesis of nanostructures[J]. Science, 1991,254(5036):1312-1319.
3. [3]
  Ulijn R. V., Smith A. M.. Designing peptide based nanomaterials[J]. Chem. Soc. Rev., 2008,37(4):664-675. doi: 10.1039/b609047h
4. [4]
  Zhao F., Ma M. L., Xu B.. Molecular hydrogels of therapeutic agents[J]. Chem. Soc. Rev., 2009,38(4):883-891. doi: 10.1039/b806410p
5. [5]
  Cui H., Webber M. J., Stupp S. I.. Self-assembly of peptide amphiphiles:from molecules to nanostructures to biomaterials[J]. Biopolymers, 2010,94(1):1-18. doi: 10.1002/bip.21328
6. [6]
  Gao Y., Yang Z., Kuang Y., Ma M. L., Li J., Zhao F., Xu B.. Enzyme-instructed self-assembly of peptide derivatives to form nanofibers and hydrogels[J]. Biopolymers, 2010,94(1):19-31. doi: 10.1002/bip.21321
7. [7]
  Gao Y., Zhao F., Wang Q., Zhang Y., Xu B.. Small peptide nanofibers as the matrices of molecular hydrogels for mimicking enzymes and enhancing the activity of enzymes[J]. Chem. Soc. Rev., 2010,39(9):3425-3433. doi: 10.1039/b919450a
8. [8]
  Woolfson D. N.. Building fibrous biomaterials from alpha-helical and collagen-like coiled-coil peptides[J]. Biopolymers, 2010,94(1):118-127. doi: 10.1002/bip.21345
9. [9]
  Yan C., Pochan D. J.. Rheological properties of peptide-based hydrogels for biomedical and other applications[J]. Chem. Soc. Rev., 2010,39(9):3528-3540.
10. [10]
  Aida T., Meijer E. W., Stupp S. I.. Functional supramolecular polymers[J]. Science, 2012,335(6070):813-817. doi: 10.1126/science.1205962
11. [11]
  Matson J. B., Stupp S. I.. Self-assembling peptide scaffolds for regenerative medicine[J]. Chem. Commun., 2012,48(1):26-33.
12. [12]
  Boekhoven J., Stupp S. I.. 25th anniversary article:supramolecular materials for regenerative medicine[J]. Adv. Mater., 2014,26(11):1642-1659. doi: 10.1002/adma.201304606
13. [13]
  Fichman G., Gazit E.. Self-assembly of short peptides to form hydrogels:design of building blocks, physical properties and technological applications[J]. Acta Biomater., 2014,10(4):1671-1682. doi: 10.1016/j.actbio.2013.08.013
14. [14]
  Fleming S., Ulijn R. V.. Design of nanostructures based on aromatic peptide amphiphiles[J]. Chem. Soc. Rev., 2014,43(23):8150-8177. doi: 10.1039/C4CS00247D
15. [15]
  Ng V. W., Chan J. M., Sardon H., Ono R. J., Garcia J. M., Yang Y. Y., Hedrick J. L.. Antimicrobial hydrogels:a new weapon in the arsenal against multidrug-resistant infections[J]. Adv. Drug. Deliver. Rev., 2014,78:46-62. doi: 10.1016/j.addr.2014.10.028
16. [16]
  Ramakers B. E., van Hest J. C., Lowik D. W.. Molecular tools for the construction of peptide-based materials[J]. Chem. Soc. Rev., 2014,43(8):2743-2756. doi: 10.1039/c3cs60362h
17. [17]
  Ren C., Zhang J., Chen M., Yang Z.. Self-assembling small molecules for the detection of important analytes[J]. Chem. Soc. Rev., 2014,43(21):7257-7266. doi: 10.1039/C4CS00161C
18. [18]
  Du X., Zhou J., Shi J., Xu B.. Supramolecular hydrogelators and hydrogels:from soft matter to molecular biomaterials[J]. Chem. Rev., 2015,115(24):13165-13307.
19. [19]
  Loo Y., Hauser C. A.. Bioprinting synthetic self-assembling peptide hydrogels for biomedical applications[J]. Biomed. Mater., 2015,11(1). doi: 10.1088/1748-6041/11/1/014103
20. [20]
  Rubert Perez C. M., Stephanopoulos N., Sur S., Lee S. S., Newcomb C., Stupp S. I.. The powerful functions of peptide-based bioactive matrices for regenerative medicine[J]. Ann. Biomed. Eng., 2015,43(3):501-514.
21. [21]
  de Leon Rodriguez L. M., Hemar Y., Cornish J., Brimble M. A.. Structure-mechanical property correlations of hydrogel forming beta-sheet peptides[J]. Chem. Soc. Rev., 2016,45(17):4797-4824. doi: 10.1039/C5CS00941C
22. [22]
  Koutsopoulos S.. Self-assembling peptide nanofiber hydrogels in tissue engineering and regenerative medicine:progress, design guidelines, and applications[J]. J. Biomed. Mater. Res. A, 2016,104(4):1002-1016.
23. [23]
  Tao K., Levin A., Adler-Abramovich L., Gazit E.. Fmoc-modified amino acids and short peptides:simple bio-inspired building blocks for the fabrication of functional materials[J]. Chem. Soc. Rev., 2016,45(14):3935-3953. doi: 10.1039/C5CS00889A
24. [24]
  Dou X. Q., Feng C. L.. Amino acids and peptide-based supramolecular hydrogels for three-dimensional cell culture[J]. Adv. Mater., 2017,29(16). doi: 10.1002/adma.201604062
25. [25]
  Eskandari S., Guerin T., Toth I., Stephenson R. J.. Recent advances in self-assembled peptides:Implications for targeted drug delivery and vaccine engineering[J]. Adv. Drug. Deliver. Rev., 2017:110-187.
26. [26]
  Singh N., Kumar M., Miravet J. F., Ulijn R. V., Escuder B.. Peptide-based molecular hydrogels as supramolecular protein mimics[J]. Chemistry, 2017,23(5):981-993. doi: 10.1002/chem.201602624
27. [27]
  Song Z., Chen X., You X., Huang K., Dhinakar A., Gu Z., Wu J.. Self-assembly of peptide amphiphiles for drug delivery:the role of peptide primary and secondary structures[J]. Biomater. Sci., 2017,5(12):2369-2380. doi: 10.1039/C7BM00730B
28. [28]
  Worthington P., Langhans S., Pochan D.. beta-hairpin peptide hydrogels for package delivery[J]. Adv. Drug. Deliv. Rev., 2017:110-136.
29. [29]
  Zhou J., Li J., Du X., Xu B.. Supramolecular biofunctional materials[J]. Biomaterials, 2017,129:1-27. doi: 10.1016/j.biomaterials.2017.03.014
30. [30]
  Zhao X., Pan F., Xu H., Yaseen M., Shan H., Hauser C. A., Zhang S., Lu J. R.. Molecular self-assembly and applications of designer peptide amphiphiles[J]. Chem. Soc. Rev., 2010,39(9):3480-3498. doi: 10.1039/b915923c
31. [31]
  Luo Z., Zhang S.. Designer nanomaterials using chiral self-assembling peptide systems and their emerging benefit for society[J]. Chem. Soc. Rev., 2012,41(13):4736-4754.
32. [32]
  Bowerman C. J., Nilsson B. L.. Self-assembly of amphipathic beta-sheet peptides:insights and applications[J]. Biopolymers, 2012,98(3):169-184. doi: 10.1002/bip.22058
33. [33]
  Draper E. R., Adams D. J.. Low-molecular-weight gels:the state of the art[J]. Chem, 2017,3(3):390-410.
34. [34]
  van Esch J. H.. We can design molecular gelators, but do we understand them?[J]. Langmuir, 2009,25(15):8392-8394. doi: 10.1021/la901720a
35. [35]
  Onuchic J. N., Luthey-Schulten Z., Wolynes P. G.. Theory of protein folding:the energy landscape perspective[J]. Annu. Rev. Phys. Chem., 1997,48:545-600.
36. [36]
  Li Y., Qin M., Cao Y., Wang W.. Designing the mechanical properties of peptide-based supramolecular hydrogels for biomedical applications[J]. Sci. China Phys. Mech., 2014,57(5):849-858. doi: 10.1007/s11433-014-5427-z
37. [37]
  Raeburn J., Zamith Cardoso A., Adams D. J.. The importance of the self-assembly process to control mechanical properties of low molecular weight hydrogels[J]. Chem. Soc. Rev., 2013,42(12):5143-5156. doi: 10.1039/c3cs60030k
38. [38]
  Mattia E., Otto S.. Supramolecular systems chemistry[J]. Nat. Nanotechnol., 2015,10(2):111-119. doi: 10.1038/nnano.2014.337
39. [39]
  Cai S. Q., Suo Z. G.. Equations of state for ideal elastomeric gels[J]. EPL, 2012,97(3). doi: 10.1209/0295-5075/97/34009
40. [40]
  Illeperuma W. R. K., Sun J. Y., Suo Z. G., Vlassak J. J.. Force and stroke of a hydrogel actuator[J]. Soft Matter, 2013,9(35):8504-8511. doi: 10.1039/c3sm51617b
41. [41]
  Hartgerink J. D., Beniash E., Stupp S. I.. Self-assembly and mineralization of peptide-amphiphile nanofibers[J]. Science, 2001,294(5547):1684-1688. doi: 10.1126/science.1063187
42. [42]
  van Bommel K. J., van der Pol C., Muizebelt I., Friggeri A., Heeres A., Meetsma A., Feringa B. L., van Esch J.. Responsive cyclohexane-based low-molecular-weight hydrogelators with modular architecture[J]. Angew. Chem. Int. Ed., 2004,43(13):1663-1667. doi: 10.1002/(ISSN)1521-3773
43. [43]
  Yokoi H., Kinoshita T., Zhang S.. Dynamic reassembly of peptide RADA16 nanofiber scaffold[J]. Proc. Natl. Acad. Sci. USA, 2005,102(24):8414-8419. doi: 10.1073/pnas.0407843102
44. [44]
  Schneider J. P., Pochan D. J., Ozbas B., Rajagopal K., Pakstis L., Kretsinger J.. Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide[J]. J. Am. Chem. Soc., 2002,124(50):15030-15037.
45. [45]
  Smith A. M., Williams R. J., Tang C., Coppo P., Collins R. F., Turner M. L., Saiani A., Ulijn R. V.. Fmoc-diphenylalanine self assembles to a hydrogel via a novel architecture based on pi-pi interlocked beta-sheets[J]. Adv. Mater., 2008,20(1):37-41. doi: 10.1002/(ISSN)1521-4095
46. [46]
  Mahler A., Reches M., Rechter M., Cohen S., Gazit E.. Rigid, self-assembled hydrogel composed of a modified aromatic dipeptide[J]. Adv. Mater., 2006,18(11):1365-1370. doi: 10.1002/(ISSN)1521-4095
47. [47]
  Ma M., Kuang Y., Gao Y., Zhang Y., Gao P., Xu B.. Aromatic-aromatic interactions induce the self-assembly of pentapeptidic derivatives in water to form nanofibers and supramolecular hydrogels[J]. J. Am. Chem. Soc., 2010,132(8):2719-2728. doi: 10.1021/ja9088764
48. [48]
  Dougherty D. A.. The cation-pi interaction[J]. Acc. Chem. Res., 2013,46(4):885-893. doi: 10.1021/ar300265y
49. [49]
  Chandler D.. Interfaces and the driving force of hydrophobic assembly[J]. Nature, 2005,437(7059):640-647. doi: 10.1038/nature04162
50. [50]
  Tsonchev S., Niece K. L., Schatz G. C., Ratner M. A., Stupp S. I.. Phase diagram for assembly of biologically-active peptide amphiphiles[J]. J. Phys. Chem. B, 2008,112(2):441-447. doi: 10.1021/jp076273z
51. [51]
  Rehm T. H., Schmuck C.. Ion-pair induced self-assembly in aqueous solvents[J]. Chem. Soc. Rev., 2010,39(10):3597-3611. doi: 10.1039/b926223g
52. [52]
  Legon A. C., Millen D. J.. Angular geometries and other properties of hydrogen-bonded dimers-a simple electrostatic interpretation of the success of the electron-pair model[J]. Chem. Soc. Rev., 1987,16(4):467-498.
53. [53]
  Knowles T. P., Fitzpatrick A. W., Meehan S., Mott H. R., Vendruscolo M., Dobson C. M., Welland M. E.. Role of intermolecular forces in defining material properties of protein nanofibrils[J]. Science, 2007,318(5858):1900-1903. doi: 10.1126/science.1150057
54. [54]
  Hunter C. A., Sanders J. K. M.. The nature of pi-pi interactions[J]. J. Am. Chem. Soc., 1990,112(14):5525-5534. doi: 10.1021/ja00170a016
55. [55]
  Ma C. D., Wang C., Acevedo-Velez C., Gellman S. H., Abbott N. L.. Modulation of hydrophobic interactions by proximally immobilized ions[J]. Nature, 2015,517(7534):347-350.
56. [56]
  Yan X., Zhu P., Li J.. Self-assembly and application of diphenylalanine-based nanostructures[J]. Chem. Soc. Rev., 2010,39(6):1877-1890. doi: 10.1039/b915765b
57. [57]
  Bell G. I.. Models for specific adhesion of cells to cells[J]. Science, 1978,200(4342):618-627. doi: 10.1126/science.347575
58. [58]
  Jaremko M., Jaremko L., Kim H. Y., Cho M. K., Schwieters C. D., Giller K., Becker S., Zweckstetter M.. Cold denaturation of a protein dimer monitored at atomic resolution[J]. Nat. Chem. Biol., 2013,9(4):264-270. doi: 10.1038/nchembio.1181
59. [59]
  Mason J. M., Arndt K. M.. Coiled coil domains:stability, specificity, and biological implications[J]. ChemBioChem, 2004,5(2):170-176.
60. [60]
  Pandya M. J., Spooner G. M., Sunde M., Thorpe J. R., Rodger A., Woolfson D. N.. Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis[J]. Biochemistry, 2000,39(30):8728-8734. doi: 10.1021/bi000246g
61. [61]
  Banwell E. F., Abelardo E. S., Adams D. J., Birchall M. A., Corrigan A., Donald A. M., Kirkland M., Serpell L. C., Butler M. F., Woolfson D. N.. Rational design and application of responsive alpha-helical peptide hydrogels[J]. Nat. Mater., 2009,8(7):596-600. doi: 10.1038/nmat2479
62. [62]
  Vepari C., Kaplan D. L.. Silk as a Biomaterial[J]. Prog. Polym. Sci., 2007,32(8-9):991-1007.
63. [63]
  Asakura T., Ohata T., Kametani S., Okushita K., Yazawa K., Nishiyama Y., Nishimura K., Aoki A., Suzuki F., Kaji H., Ulrich A. S., Williamson M. P.. Intermolecular packing in B. mori Silk fibroin:multinuclear NMR Study of the model peptide (Ala-Gly)(15) Defines a heterogeneous antiparallel antipolar mode of assembly in the silk ò form[J]. Macromolecules, 2015,48(1):28-36. doi: 10.1021/ma502191g
64. [64]
  Altman G. H., Diaz F., Jakuba C., Calabro T., Horan R. L., Chen J. S., Lu H., Richmond J., Kaplan D. L.. Silk-based biomaterials[J]. Biomaterials., 2003,24(3):401-416. doi: 10.1016/S0142-9612(02)00353-8
65. [65]
  Zhang S., Holmes T., Lockshin C., Rich A.. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane[J]. Proc. Natl. Acad. Sci. USA., 1993,90(8):3334-3338. doi: 10.1073/pnas.90.8.3334
66. [66]
  Collier J. H., Hu B. H., Ruberti J. W., Zhang J., Shum P., Thompson D. H., Messersmith P. B.. Thermally and photochemically triggered self-assembly of peptide hydrogels[J]. J. Am. Chem. Soc., 2001,123(38):9463-9464. doi: 10.1021/ja011535a
67. [67]
  Bowerman C. J., Liyanage W., Federation A. J., Nilsson B. L.. Tuning beta-sheet peptide self-assembly and hydrogelation behavior by modification of sequence hydrophobicity and aromaticity[J]. Biomacromolecules, 2011,12(7):2735-2745.
68. [68]
  Lee N. R., Bowerman C. J., Nilsson B. L.. Effects of varied sequence pattern on the self-assembly of amphipathic peptides[J]. Biomacromolecules., 2013,14(9):3267-3277. doi: 10.1021/bm400876s
69. [69]
  Dong H., Paramonov S. E., Aulisa L., Bakota E. L., Hartgerink J. D.. Self-assembly of multidomain peptides:balancing molecular frustration controls conformation and nanostructure[J]. J. Am. Chem. Soc., 2007,129(41):12468-12472. doi: 10.1021/ja072536r
70. [70]
  Yang Z. M., Xu K. M., Guo Z. F., Guo Z. H., Xu B.. Intracellular enzymatic formation of nanofibers results in hydrogelation and regulated cell death[J]. Adv. Mater., 2007,19(20):3152-3156. doi: 10.1002/adma.200701971
71. [71]
  Yang Z. M., Ho P. L., Liang G. L., Chow K. H., Wang Q. G., Cao Y., Guo Z. H., Xu B.. Using beta-lactamase to trigger supramolecular hydrogelation[J]. J. Am. Chem. Soc., 2007,129(2):266-267. doi: 10.1021/ja0675604
72. [72]
  Zhang Y., Kuang Y., Gao Y., Xu B.. Versatile small-molecule motifs for self-assembly in water and the formation of biofunctional supramolecular hydrogels[J]. Langmuir, 2011,27(2):529-537. doi: 10.1021/la1020324
73. [73]
  Wang H. M., Yang C. H., Tan M., Wang L., Kong D. L., Yang Z. M.. A structure-gelation ability study in a short peptide-based nSuper Hydrogelatoro system[J]. Soft Matter, 2011,7(8):3897-3905. doi: 10.1039/c0sm01405b
74. [74]
  Liang C. H., Zheng D. B., Shi F., Xu T. Y., Yang C. H., Liu J. F., Wang L., Yang Z. M.. Enzyme-assisted peptide folding, assembly and anti-cancer properties[J]. Nanoscale, 2017,9(33):11987-11993. doi: 10.1039/C7NR04370H
75. [75]
  Wang Z. Y., Liang C. H., Shi F., He T., Gong C. Y., Wang L., Yang Z. M.. Cancer vaccines using supramolecular hydrogels of NSAID-modified peptides as adjuvants abolish tumorigenesis[J]. Nanoscale, 2017,9(37):14058-14064. doi: 10.1039/C7NR04990K
76. [76]
  Zhan J., Cai Y. B., Ji S. L., He S. S., Cao Y., Ding D., Wang L., Yang Z. M.. Spatiotemporal control of supramolecular self-assembly and function[J]. ACS Appl. Mater. Interfaces, 2017,9(11):10012-10018.
77. [77]
  Cai Y. B., Shen H. S., Zhan J., Lin M. L., Dai L. H., Ren C. H., Shi Y., Liu J. F., Gao J., Yang Z. M.. Supramolecular "Trojan Horse" for nuclear delivery of dual anticancer drugs[J]. J. Am. Chem. Soc., 2017,139(8):2876-2879. doi: 10.1021/jacs.6b12322
78. [78]
  Wang H. M., Luo Z., Wang Y. C. Z., He T., Yang C. B., Ren C. H., Ma L. S., Gong C. Y., Li X. Y., Yang Z. M.. Enzyme-catalyzed formation of supramolecular hydrogels as promising vaccine adjuvants[J]. Adv. Funct. Mater., 2016,26(11):1822-1829.
79. [79]
  Zhang X. L., Dong C. M., Huang W. Y., Wang H. M., Wang L., Ding D., Zhou H., Long J. F., Wang T. L., Yang Z. M.. Rational design of a photo-responsive UVR8-derived protein and a self-assembling peptide-protein conjugate for responsive hydrogel formation[J]. Nanoscale, 2015,7(40):16666-16670. doi: 10.1039/C5NR05213K
80. [80]
  Zhang J. W., Ou C. W., Shi Y., Wang L., Chen M. S., Yang Z. M.. Visualized detection of melamine in milk by supramolecular hydrogelations[J]. Chem. Commun., 2014,50(85):12873-12876. doi: 10.1039/C4CC05826G
81. [81]
  Hai Z. J., Li J. D., Wu J. J., Xu J. C., Liang G. L.. Alkaline phosphatase-triggered simultaneous hydrogelation and chemiluminescence[J]. J. Am. Chem. Soc., 2017,139(3):1041-1044. doi: 10.1021/jacs.6b11041
82. [82]
  Wu C. F., Zheng Z., Guo Y. N., Tian C. L., Xue Q., Liang G. L.. Fluorine substitution enhances the self-assembling ability of hydrogelators[J]. Nanoscale, 2017,9(32):11429-11433.
83. [83]
  Zheng Z., Chen P. Y., Xie M. L., Wu C. F., Luo Y. F., Wang W. T., Jiang J., Liang G. L.. Cell environment-differentiated self-assembly of nanofibers[J]. J. Am. Chem. Soc., 2016,138(35):11128-11131. doi: 10.1021/jacs.6b06903
84. [84]
  Ding Y., Li Y., Qin M., Cao Y., Wang W.. Photo-cross-linking approach to engineering small tyrosine-containing peptide hydrogels with enhanced mechanical stability[J]. Langmuir, 2013,29(43):13299-13306. doi: 10.1021/la4029639
85. [85]
  Xue B., Qin M., Wang T. K., Wu J. H., Luo D. J., Jiang Q., Li Y., Cao Y., Wang W.. Electrically controllable actuators based on supramolecular peptide hydrogels[J]. Adv. Funct. Mater., 2016,26(48):9053-9062. doi: 10.1002/adfm.v26.48
86. [86]
  Li Y., Wang L.. Removing organic dyes by using a small peptide hydrogel[J]. Chem. Lett., 2016,45(11):1253-1255. doi: 10.1246/cl.160597
87. [87]
  Cheng W., Li Y.. Peptide hydrogelation triggered by enzymatic induced pH switch[J]. Sci. China Phys. Mech., 2016,59(7):678-711.
88. [88]
  Newcomb C. J., Bitton R., Velichko Y. S., Snead M. L., Stupp S. I.. The role of nanoscale architecture in supramolecular templating of biomimetic hydroxyapatite mineralization[J]. Small, 2012,8(14):2195-2202.
89. [89]
  Pashuck E. T., Cui H. G., Stupp S. I.. Tuning supramolecular rigidity of peptide fibers through molecular structure[J]. J. Am. Chem. Soc., 2010,132(17):6041-6046. doi: 10.1021/ja908560n
90. [90]
  da Silva R. M., van der Zwaag D., Albertazzi L., Lee S. S., Meijer E. W., Stupp S. I.. Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres[J]. Nat. Commun., 2016,7. doi: 10.1038/ncomms11561
91. [91]
  Ortony J. H., Qiao B., Newcomb C. J., Keller T. J., Palmer L. C., Deiss-Yehiely E., Olvera de la Cruz M., Han S., Stupp S. I.. Water Dynamics from the Surface to the Interior of a Supramolecular Nanostructure[J]. J. Am. Chem. Soc., 2017,139(26):8915-8921. doi: 10.1021/jacs.7b02969
92. [92]
  Pochan D. J., Schneider J. P., Kretsinger J., Ozbas B., Rajagopal K., Haines L.. Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide[J]. J. Am. Chem. Soc., 2003,125(39):11802-11803. doi: 10.1021/ja0353154
93. [93]
  Lamm M. S., Rajagopal K., Schneider J. P., Pochan D. J.. Laminated morphology of nontwisting beta-sheet fibrils constructed via peptide self-assembly[J]. J. Am. Chem. Soc., 2005,127(47):16692-16700.
94. [94]
  Salick D. A., Pochan D. J., Schneider J. P.. Design of an injectable beta-hairpin peptide hydrogel that kills methicillin-resistant staphylococcus aureus[J]. Adv. Mater., 2009,21(41):4120-4123.
95. [95]
  Rughani R. V., Salick D. A., Lamm M. S., Yucel T., Pochan D. J., Schneider J.P.. Folding, self-assembly, and bulk material properties of a de novo designed three-stranded beta-sheet hydrogel[J]. Biomacromolecules, 2009,10(5):1295-1304. doi: 10.1021/bm900113z
96. [96]
  Rajagopal K., Lamm M. S., Haines-Butterick L. A., Pochan D. J., Schneider J. P.. Tuning the pH Responsiveness of beta-Hairpin peptide folding, self-assembly, and hydrogel material formation[J]. Biomacromolecules, 2009,10(9):2619-2625. doi: 10.1021/bm900544e
97. [97]
  Ding B. Y., Li Y., Qin M., Ding Y., Cao Y., Wang W.. Two approaches for the engineering of homogeneous small-molecule hydrogels[J]. Soft Matter, 2013,9(18):4672-4680. doi: 10.1039/c3sm50324k
98. [98]
  Wang J., Liu K., Xing R., Yan X.. Peptide self-assembly:thermodynamics and kinetics[J]. Chem. Soc. Rev., 2016,45(20):5589-5604. doi: 10.1039/C6CS00176A
99. [99]
  Sasselli I. R., Halling P. J., Ulijn R. V., Tuttle T.. Supramolecular fibers in gels can be at thermodynamic equilibrium:a simple packing model reveals preferential fibril formation versus crystallization[J]. ACS Nano, 2016,10(2):2661-2668. doi: 10.1021/acsnano.5b07690
100. [100]
  Adams D. J., Morris K., Chen L., Serpell L. C., Bacsa J., Day G. M.. The delicate balance between gelation and crystallisation:structural and computational investigations[J]. Soft Matter, 2010,6(17):4144-4156. doi: 10.1039/c0sm00409j
101. [101]
  Lan Y., Corradini M. G., Weiss R. G., Raghavan S. R., Rogers M. A.. To gel or not to gel:correlating molecular gelation with solvent parameters[J]. Chem. Soc. Rev., 2015,44(17):6035-6058. doi: 10.1039/C5CS00136F
102. [102]
  Raynal M., Bouteiller L.. Organogel formation rationalized by Hansen solubility parameters[J]. Chem. Commun., 2011,47(29):8271-8273. doi: 10.1039/c1cc13244j
103. [103]
  Lloyd G. O., Steed J. W.. Anion-tuning of supramolecular gel properties[J]. Nat. Chem., 2009,1(6):437-442. doi: 10.1038/nchem.283
104. [104]
  Massi F., Straub J. E.. Energy landscape theory for Alzheimer's amyloid beta-peptide fibril elongation[J]. Proteins, 2001,42(2):217-229.
105. [105]
  Straub J. E., Thirumalai D.. Toward a molecular theory of early and late events in monomer to amyloid fibril formation[J]. Annu. Rev. Phys. Chem., 2011,62:437-463. doi: 10.1146/annurev-physchem-032210-103526
106. [106]
  Lansbury P. T.. A reductionist view of Alzheimer's disease[J]. Acc. Chem. Res., 1996,29(7):317-321. doi: 10.1021/ar950159u
107. [107]
  Hall D., Hirota N., Dobson C. M.. A toy model for predicting the rate of amyloid formation from unfolded protein[J]. J. Mol. Biol., 2005,351(1):195-205. doi: 10.1016/j.jmb.2005.05.013
108. [108]
  Lomakin A., Chung D. S., Benedek G. B., Kirschner D. A., Teplow D. B.. On the nucleation and growth of amyloid beta-protein fibrils:detection of nuclei and quantitation of rate constants[J]. Proc. Natl. Acad. Sci. USA, 1996,93(3):1125-1129. doi: 10.1073/pnas.93.3.1125
109. [109]
  Lomakin A., Teplow D. B., Kirschner D. A., Benedek G. B.. Kinetic theory of fibrillogenesis of amyloid beta-protein[J]. Proc. Natl. Acad. Sci. USA., 1997,94(15):7942-7947. doi: 10.1073/pnas.94.15.7942
110. [110]
  Gibson T. J., Murphy R. M.. Design of peptidyl compounds that affect beta-amyloid aggregation:importance of surface tension and context[J]. Biochemistry, 2005,44(24):8898-8907. doi: 10.1021/bi050225s
111. [111]
  Knowles T. P., Waudby C. A., Devlin G. L., Cohen S. I., Aguzzi A., Vendruscolo M., Terentjev E. M., Welland M. E., Dobson C. M.. An analytical solution to the kinetics of breakable filament assembly[J]. Science, 2009,326(5959):1533-1537. doi: 10.1126/science.1178250
112. [112]
  Harper J. D., Wong S. S., Lieber C. M., Lansbury P. T.. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy[J]. Chem. Biol., 1997,4(2):119-125. doi: 10.1016/S1074-5521(97)90255-6
113. [113]
  Walsh D. M., Lomakin A., Benedek G. B., Condron M. M., Teplow D. B.. Amyloid beta-protein fibrillogenesis[J]. Detection of a protofibrillar intermediate. J. Biol. Chem., 1997,272(35):22364-22372.
114. [114]
  Arosio P., Knowles T. P. J., Linse S.. On the lag phase in amyloid fibril formation[J]. Phys. Chem. Chem. Phys., 2015,17(12):7606-7618. doi: 10.1039/C4CP05563B
115. [115]
  Fletcher N. L., Lockett C. V., Dexter A. F.. A pH-responsive coiled-coil peptide hydrogel[J]. Soft Matter, 2011,7(21):10210-10218.
116. [116]
  Massi F., Straub J. E.. Energy landscape theory for Alzheimer's amyloid beta-peptide fibril elongation[J]. Proteins, 2001,42(2):217-229. doi: 10.1002/(ISSN)1097-0134
117. [117]
  Ahmed S., Pramanik B., Sankar K. N. A., Srivastava A., Singha N., Dowari P., Srivastava A., Mohanta K., Debnath A., Das D.. Solvent assisted tuning of morphology of a peptide-perylenediimide conjugate: helical fibers to nano-rings and their differential semiconductivity[J]. Sci. Rep., 2017,7(1). doi: 10.1038/s41598-017-09730-z
118. [118]
  Tian Y., Zhang H. V., Kiick K. L., Saven J. G., Pochan D. J.. Transition from disordered aggregates to ordered lattices: kinetic control of the assembly of a computationally designed peptide[J]. Org. Biomol. Chem., 2017,15(29):6109-6118. doi: 10.1039/C7OB01197K
119. [119]
  Wang Y., Huang R., Qi W., Wu Z., Su R., He Z.. Kinetically controlled self-assembly of redox-active ferrocene-diphenylalanine: from nanospheres to nanofibers[J]. Nanotechnology, 2013. doi: 10.1088/0957-4484/24/46/465603
120. [120]
  Heuser T., Weyandt E., Walther A.. Biocatalytic feedback-driven temporal programming of self-regulating peptide hydrogels[J]. Angew. Chem. Int. Ed., 2015,54(45):13258-13262. doi: 10.1002/anie.201505013
121. [121]
  Conte M. P., Singh N., Sasselli I. R., Escuder B., Ulijn R. V.. Metastable hydrogels from aromatic dipeptides[J]. Chem. Commun., 2016,52(96):13889-13892.
122. [122]
  Debnath S., Roy S., Ulijn R. V.. Peptide nanofibers with dynamic instability through nonequilibrium biocatalytic assembly[J]. J. Am. Chem. Soc., 2013,135(45):16789-16792. doi: 10.1021/ja4086353
123. [123]
  Williams R. J., Smith A. M., Collins R., Hodson N., Das A. K., Ulijn R. V.. Enzyme-assisted self-assembly under thermodynamic control[J]. Nat. Nanotechnol., 2009,4(1):19-24. doi: 10.1038/nnano.2008.378
124. [124]
  Adams D. J., Butler M. F., Frith W. J., Kirkland M., Mullen L., Sanderson P.. A new method for maintaining homogeneity during liquid-hydrogel transitions using low molecular weight hydrogelators[J]. Soft Matter, 2009,5(9):1856-1862. doi: 10.1039/b901556f
125. [125]
  Ferreiro D. U., Komives E. A., Wolynes P. G.. Frustration in biomolecules[J]. Q. Rev. Biophys., 2014,47(4):285-363. doi: 10.1017/S0033583514000092
126. [126]
  Wolynes P.G.. Evolution, energy landscapes and the paradoxes of protein folding[J]. Biochimie., 2015,119:218-230. doi: 10.1016/j.biochi.2014.12.007
127. [127]
  Levy Y., Onuchic J. N.. Mechanisms of protein assembly: lessons from minimalist models[J]. Acc. Chem. Res., 2006,39(2):135-142. doi: 10.1021/ar040204a
128. [128]
  Friedel M., Shea J. E.. Self-assembly of peptides into a beta-barrel motif[J]. J. Chem. Phys., 2004,120(12):5809-5823. doi: 10.1063/1.1649934
129. [129]
  Schmidt M., Rohou A., Lasker K., Yadav J. K., Schiene-Fischer C., Fandrich M., Grigorieff N.. Peptide dimer structure in an Abeta(1-42) fibril visualized with cryo-EM[J]. Proc. Natl. Acad. Sci. USA, 2015,112(38):11858-11863. doi: 10.1073/pnas.1503455112
130. [130]
  Pinotsi D., Kaminski Schierle G. S., Kaminski C. F.. Optical Super-resolution imaging of beta-amyloid aggregation in vitro and in vivo: method and techniques[J]. Method. Mol. Biol., 2016,1303:125-141.
131. [131]
  Milhiet P. E., Yamamoto D., Berthoumieu O., Dosset P., Le Grimellec C., Verdier J. M., Marchal S., Ando T.. Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy[J]. PLoS One., 2010,5(10). doi: 10.1371/journal.pone.0013240
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