請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/21712
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 王勝仕 | |
dc.contributor.author | Shang-Yu Shen | en |
dc.contributor.author | 沈尚諭 | zh_TW |
dc.date.accessioned | 2021-06-08T03:43:36Z | - |
dc.date.copyright | 2019-07-02 | |
dc.date.issued | 2019 | |
dc.date.submitted | 2019-06-05 | |
dc.identifier.citation | 1. Kumar, R. and B.R. Singh, Introduction to Protein Folding, in Protein Toxins in Modeling Biochemistry. 2016, Springer International Publishing: Cham. p. 5-28.
2. Wu, C.H., et al., Protein family classification and functional annotation. Computational Biology and Chemistry, 2003. 27(1): p. 37-47. 3. ; Available from: http://www.peptidesguide.com/peptide-bond.html. 4. Banerjee, J., E. Radvar, and H.S. Azevedo, 10 - Self-assembling peptides and their application in tissue engineering and regenerative medicine, in Peptides and Proteins as Biomaterials for Tissue Regeneration and Repair, M.A. Barbosa and M.C.L. Martins, Editors. 2018, Woodhead Publishing. p. 245-281. 5. Pelley, J.W., 3 - Protein Structure and Function, in Elsevier's Integrated Biochemistry, J.W. Pelley, Editor. 2007, Mosby: Philadelphia. p. 19-28. 6. Collinge, J., Prion Diseases of Humans and Animals: Their Causes and Molecular Basis. Annual Review of Neuroscience, 2001. 24(1): p. 519-550. 7. Ouellette, R.J. and J.D. Rawn, 14 - Amino Acids, Peptides, and Proteins, in Principles of Organic Chemistry, R.J. Ouellette and J.D. Rawn, Editors. 2015, Elsevier: Boston. p. 371-396. 8. Ptitsyn, O.B., Structures of folding intermediates. Current Opinion in Structural Biology, 1995. 5(1): p. 74-78. 9. Schäfer, H., et al., Entropy calculations on the molten globule state of a protein: Side-chain entropies of α-lactalbumin. Proteins: Structure, Function, and Bioinformatics, 2002. 46(2): p. 215-224. 10. Dobson, C.M., Protein folding and misfolding. Nature, 2003. 426(6968): p. 884. 11. Narhi, L.O., et al., Classification of protein aggregates. Journal of pharmaceutical sciences, 2012. 101(2): p. 493-498. 12. Stefani, M. and C.M. Dobson, Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. Journal of molecular medicine, 2003. 81(11): p. 678-699. 13. Arosio, P., T.P.J. Knowles, and S. Linse, On the lag phase in amyloid fibril formation. Physical Chemistry Chemical Physics, 2015. 17(12): p. 7606-7618. 14. Chaturvedi, S.K., et al., Protein misfolding and aggregation: mechanism, factors and detection. Process Biochemistry, 2016. 51(9): p. 1183-1192. 15. Makin, O.S. and L.C. Serpell, Structures for amyloid fibrils. The FEBS Journal, 2005. 272(23): p. 5950-5961. 16. Goldsbury, C.S., et al., Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors. Journal of Structural Biology, 2000. 130(2): p. 217-231. 17. Serpell, L., Amyloid structure. Essays in biochemistry, 2014. 56: p. 1-10. 18. Mohammadian, M. and A. Madadlou, Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution. Food Hydrocolloids, 2016. 52: p. 221-230. 19. Van Der Linden, E., Innovations with protein nano-fibres. World's Poultry Science Journal, 2006. 62(3): p. 439-442. 20. Liu, G. and Q. Zhong, Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein. Biomacromolecules, 2013. 14(7): p. 2146-2153. 21. Zou, Y., et al., Effect of dextran glycation on nanofibril assembly of soya β-conglycinin at pH 2.0 and the pH stability of nanofibrils. Vol. 51. 2016. 22. Tang, C.-H. and C.-S. Wang, Formation and Characterization of Amyloid-like Fibrils from Soy β-Conglycinin and Glycinin. Journal of Agricultural and Food Chemistry, 2010. 58(20): p. 11058-11066. 23. Mohammadian, M. and A. Madadlou, Cold-set hydrogels made of whey protein nanofibrils with different divalent cations. Int J Biol Macromol, 2016. 89: p. 499-506. 24. Meza, B.E., R.A. Verdini, and A.C. Rubiolo, Viscoelastic behaviour of heat-treated whey protein concentrate suspensions. Food Hydrocolloids, 2009. 23(3): p. 661-666. 25. Loveday, S., et al., β-Lactoglobulin Nanofibrils: Effect of Temperature on Fibril Formation Kinetics, Fibril Morphology and the Rheological Properties of Fibril Dispersions. 2012. 26. Zhang, Y.-H., L.-H. Huang, and Z.-C. Wei, Effects of additional fibrils on structural and rheological properties of rice bran albumin solution and gel. Vol. 239. 2014. 971-978. 27. Lasse, M., et al., Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white. Food Chem, 2016. 192: p. 491-8. 28. Bateman, L., A. Ye, and H. Singh, In Vitro Digestion of β-Lactoglobulin Fibrils Formed by Heat Treatment at Low pH. Journal of Agricultural and Food Chemistry, 2010. 58(17): p. 9800-9808. 29. Hauser, C.A., S. Maurer-Stroh, and I.C. Martins, Amyloid-based nanosensors and nanodevices. Chem Soc Rev, 2014. 43(15): p. 5326-45. 30. Sasso, L., et al., Versatile multi-functionalization of protein nanofibrils for biosensor applications. Nanoscale, 2014. 6(3): p. 1629-34. 31. Pilkington, S.M., et al., Amyloid fibrils as a nanoscaffold for enzyme immobilization. Biotechnol Prog, 2010. 26(1): p. 93-100. 32. Ding, M. and X. Shi, Molecular mechanisms of Cr(VI)-induced carcinogenesis. Molecular and Cellular Biochemistry, 2002. 234(1): p. 293-300. 33. Leung, W.-H., et al., An Amyloid-Fibril-Based Colorimetric Nanosensor for Rapid and Sensitive Chromium(VI) Detection. ChemPlusChem, 2013. 78(12): p. 1440-1445. 34. Willems, G.J., et al., The interaction of chromium(VI), chromium(III) and chromium(II) with diphenylcarbazide, diphenylcarbazone and diphenylcarbadiazone. Analytica Chimica Acta, 1977. 88(2): p. 345-352. 35. Wu, X., et al., Amyloid-graphene oxide as immobilization platform of Au nanocatalysts and enzymes for improved glucose-sensing activity. J Colloid Interface Sci, 2017. 490: p. 336-342. 36. Fu, F. and Q. Wang, Removal of heavy metal ions from wastewaters: A review. Journal of Environmental Management, 2011. 92(3): p. 407-418. 37. Ghosh, P., A. Samanta, and S. Ray, Reduction of COD and removal of Zn2+ from rayon industry wastewater by combined electro-Fenton treatment and chemical precipitation. Vol. 266. 2011. 213-217. 38. Inglezakis, V.J., et al., Removal of Pb(II) from aqueous solutions by using clinoptilolite and bentonite as adsorbents. Desalination, 2007. 210(1): p. 248-256. 39. Robinson, T., et al., Remediation of dyes in textile effluent: a critical review on current treatment technologies with a proposed alternative. Bioresource Technology, 2001. 77(3): p. 247-255. 40. Pirkarami, A. and M.E. Olya, Removal of dye from industrial wastewater with an emphasis on improving economic efficiency and degradation mechanism. Journal of Saudi Chemical Society, 2017. 21: p. S179-S186. 41. O’Neill, C., et al., Colour in textile effluents – sources, measurement, discharge consents and simulation: a review. Journal of Chemical Technology & Biotechnology, 1999. 74(11): p. 1009-1018. 42. Rufo, C.M., et al., Short peptides self-assemble to produce catalytic amyloids. Nature chemistry, 2014. 6(4): p. 303-309. 43. Leung, W.-H., W.-H. Lo, and P.-H. Chan, Amyloid fibrils as rapid and efficient nano-biosorbents for removal of dye pollutants. RSC Advances, 2015. 5(109): p. 90022-90030. 44. Shin, H., S. Jo, and A.G. Mikos, Biomimetic materials for tissue engineering. Biomaterials, 2003. 24(24): p. 4353-4364. 45. Drury, J.L. and D.J. Mooney, Hydrogels for tissue engineering: scaffold design variables and applications. Biomaterials, 2003. 24(24): p. 4337-4351. 46. Ullah, F., et al., Classification, processing and application of hydrogels: A review. Materials Science and Engineering: C, 2015. 57: p. 414-433. 47. Bahram, M., N. Mohseni, and M. Moghtader, An introduction to hydrogels and some recent applications, in Emerging concepts in analysis and applications of hydrogels. 2016, IntechOpen. 48. Augst, A.D., H.J. Kong, and D.J. Mooney, Alginate Hydrogels as Biomaterials. Macromolecular Bioscience, 2006. 6(8): p. 623-633. 49. Theocharis, A.D., et al., Extracellular matrix structure. Advanced Drug Delivery Reviews, 2016. 97: p. 4-27. 50. Shah, A.L.R.a.R.N., Protein-Based Hydrogels, in Polymeric Hydrogels as Smart Biomaterials, S. Kalia, Editor. 2016, Springer International Publishing. p. 73-104. 51. wang, Y., et al., 14 - Hydrogel particles and other novel protein-based methods for food ingredient and nutraceutical delivery systems, in Encapsulation Technologies and Delivery Systems for Food Ingredients and Nutraceuticals, N. Garti and D.J. McClements, Editors. 2012, Woodhead Publishing. p. 412-450. 52. Gosal, W.S., A.H. Clark, and S.B. Ross-Murphy, Fibrillar β-Lactoglobulin Gels: Part 1. Fibril Formation and Structure. Biomacromolecules, 2004. 5(6): p. 2408-2419. 53. Nieuwland, M., et al., Relating water holding of ovalbumin gels to aggregate structure. Food Hydrocolloids, 2016. 52: p. 87-94. 54. Jafari, S.M., 1 - An overview of nanoencapsulation techniques and their classification, in Nanoencapsulation Technologies for the Food and Nutraceutical Industries, S.M. Jafari, Editor. 2017, Academic Press. p. 1-34. 55. Snyders, R., et al., Mechanical and microstructural properties of hybrid poly(ethylene glycol)–soy protein hydrogels for wound dressing applications. Journal of Biomedical Materials Research Part A, 2007. 83A(1): p. 88-97. 56. Loveday, S.M., et al., Whey protein nanofibrils: Kinetic, rheological and morphological effects of group IA and IIA cations. International Dairy Journal, 2012. 26(2): p. 133-140. 57. Gunasekaran, S., S. Ko, and L. Xiao, Use of whey proteins for encapsulation and controlled delivery applications. Journal of Food Engineering, 2007. 83(1): p. 31-40. 58. Zand-Rajabi, H. and A. Madadlou, Citric acid cross-linking of heat-set whey protein hydrogel influences its textural attributes and caffeine uptake and release behaviour. International Dairy Journal, 2016. 61: p. 142-147. 59. Betz, M. and U. Kulozik, Whey protein gels for the entrapment of bioactive anthocyanins from bilberry extract. International Dairy Journal, 2011. 21(9): p. 703-710. 60. Ozel, B., et al., Polysaccharide blended whey protein isolate-(WPI) hydrogels: A physicochemical and controlled release study. Food Hydrocolloids, 2017. 71: p. 35-46. 61. Abaee, A. and A. Madadlou, Niosome-loaded cold-set whey protein hydrogels. Food Chem, 2016. 196: p. 106-13. 62. Somchue, W., et al., Encapsulation of α-tocopherol in protein-based delivery particles. Food Research International, 2009. 42(8): p. 909-914. 63. Remondetto, G.E., P. Paquin, and M. Subirade, Cold Gelation of β-lactoglobulin in the Presence of Iron. Journal of Food Science, 2002. 67(2): p. 586-595. 64. Martin, A. and G. A H de Jong, Enhancing the in vitro Fe2+ bio-accessibility using ascorbate and cold-set whey protein gel particles. Vol. 92. 2012. 133-149. 65. Onsekizoglu Bagci, P. and S. Gunasekaran, Iron-encapsulated cold-set whey protein isolate gel powder - Part 1: Optimisation of preparation conditions andin vitroevaluation. International Journal of Dairy Technology, 2017. 70(1): p. 127-136. 66. Remondetto, G.E., E. Beyssac, and M. Subirade, Iron Availability from Whey Protein Hydrogels: An in Vitro Study. Journal of Agricultural and Food Chemistry, 2004. 52(26): p. 8137-8143. 67. da Silva, M.V., J.M.P.Q. Delgado, and M.P. Gonçalves, Impact of MG2+and Tara Gum Concentrations on Flow and Textural Properties of WPI Solutions and Cold-Set Gels. International Journal of Food Properties, 2010. 13(5): p. 972-982. 68. Yamul, D.K. and C.E. Lupano, Properties of gels from whey protein concentrate and honey at different pHs. Food Research International, 2003. 36(1): p. 25-33. 69. Iemma, F., et al., pH-sensitive hydrogels based on bovine serum albumin for oral drug delivery. Int J Pharm, 2006. 312(1-2): p. 151-7. 70. Wang, K., G. Buschle-Diller, and Y. Wu, Thermoresponsive hydrogels from BSA esterified with low molecular weight PEG. Journal of Applied Polymer Science, 2014. 131(20): p. n/a-n/a. 71. Tada, D., et al., Drug release from hydrogel containing albumin as crosslinker. J Biosci Bioeng, 2005. 100(5): p. 551-5. 72. Egan, T., et al., Cold-set whey protein microgels as pH modulated immobilisation matrices for charged bioactives. Food Chem, 2014. 156: p. 197-203. 73. Caillard, R., et al., Characterization of amino cross-linked soy protein hydrogels. J Food Sci, 2008. 73(5): p. C283-91. 74. Reddy, N. and Y. Yang, Potential of plant proteins for medical applications. Trends in Biotechnology, 2011. 29(10): p. 490-498. 75. Chien, K.B., E.J. Chung, and R.N. Shah, Investigation of soy protein hydrogels for biomedical applications: Materials characterization, drug release, and biocompatibility. Journal of Biomaterials Applications, 2013. 28(7): p. 1085-1096. 76. Ding, X. and P. Yao, Soy Protein/Soy Polysaccharide Complex Nanogels: Folic Acid Loading, Protection, and Controlled Delivery. Langmuir, 2013. 29(27): p. 8636-8644. 77. Song, F. and L.-M. Zhang, Gelation Modification of Soy Protein Isolate by a Naturally Occurring Cross-Linking Agent and Its Potential Biomedical Application. Industrial & Engineering Chemistry Research, 2009. 48(15): p. 7077-7083. 78. Caillard, R., M.A. Mateescu, and M. Subirade, Maillard-Type Cross-Linked Soy Protein Hydrogels as Devices for the Release of Ionic Compounds: An In Vitro Study. Food Research International, 2010. 43(10): p. 2349-2355. 79. Hu, H., et al., Effect of ultrasound pre-treatment on formation of transglutaminase-catalysed soy protein hydrogel as a riboflavin vehicle for functional foods. Journal of Functional Foods, 2015. 19: p. 182-193. 80. Maltais, A., G.E. Remondetto, and M. Subirade, Soy protein cold-set hydrogels as controlled delivery devices for nutraceutical compounds. Food Hydrocolloids, 2009. 23(7): p. 1647-1653. 81. Liu, Y., et al., Numerical and experimental investigation of upsetting with ultrasonic vibration of pure copper cone tip. Ultrasonics, 2013. 53(3): p. 803-807. 82. Liu, Y., Y. Cui, and M. Liao, pH- and temperature-responsive IPN hydrogels based on soy protein and poly(N-isopropylacrylamide-co-sodium acrylate). Journal of Applied Polymer Science, 2014. 131(2). 83. Liu, Y., et al., Synthesis, characterization, and drug release behaviour of novel soy protein/poly(acrylic acid) IPN hydrogels. Iranian Polymer Journal (English Edition), 2009. 18(4): p. 339-348. 84. Liu, J., et al., Soy protein-based polyethylenimine hydrogel and its high selectivity for copper ion removal in wastewater treatment. Journal of Materials Chemistry A, 2017. 5(8): p. 4163-4171. 85. Berkland, C., et al., Microsphere size, precipitation kinetics and drug distribution control drug release from biodegradable polyanhydride microspheres. Journal of Controlled Release, 2004. 94(1): p. 129-141. 86. Singh, M.N., et al., Microencapsulation: A promising technique for controlled drug delivery. Research in pharmaceutical sciences, 2010. 5(2): p. 65-77. 87. Ansarifar, E., et al., Novel multilayer microcapsules based on soy protein isolate fibrils and high methoxyl pectin: Production, characterization and release modeling. International Journal of Biological Macromolecules, 2017. 97: p. 761-769. 88. Sagis, L.M.C., et al., Polymer Microcapsules with a Fiber-Reinforced Nanocomposite Shell. Langmuir, 2008. 24(5): p. 1608-1612. 89. Yow, H.N. and A.F. Routh, Formation of liquid core–polymer shell microcapsules. Soft Matter, 2006. 2(11): p. 940-949. 90. Serfert, Y., Characterisation and use of β-lactoglobulin fibrils for microencapsulation of lipophilic ingredients and oxidative stability thereof. Journal of food engineering, 2014. v. 143: p. pp. 53-61-2014 v.143. 91. Ng, S.-K., et al., Development of a palm olein oil-in-water (o/w) emulsion stabilized by a whey protein isolate nanofibrils-alginate complex. LWT - Food Science and Technology, 2017. 82: p. 311-317. 92. Gonzalez-Jordan, A., T. Nicolai, and L. Benyahia, Influence of the Protein Particle Morphology and Partitioning on the Behavior of Particle-Stabilized Water-in-Water Emulsions. Langmuir, 2016. 32(28): p. 7189-7197. 93. Gao, Z., et al., Edible Pickering emulsion stabilized by protein fibrils. Part 1: Effects of pH and fibrils concentration. LWT - Food Science and Technology, 2017. 76: p. 1-8. 94. Gao, Z., et al., Edible Pickering emulsion stabilized by protein fibrils: Part 2. Effect of dipalmitoyl phosphatidylcholine (DPPC). Food Hydrocolloids, 2017. 71: p. 245-251. 95. Jung, J.-M., D.Z. Gunes, and R. Mezzenga, Interfacial Activity and Interfacial Shear Rheology of Native β-Lactoglobulin Monomers and Their Heat-Induced Fibers. Langmuir, 2010. 26(19): p. 15366-15375. 96. Dickinson, E., Biopolymer-based particles as stabilizing agents for emulsions and foams. Food Hydrocolloids, 2017. 68: p. 219-231. 97. Song, Y., et al., Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces. Nature Communications, 2016. 7: p. 12934. 98. Beckman, C.H., Phenolic-storing cells: keys to programmed cell death and periderm formation in wilt disease resistance and in general defence responses in plants? Physiological and Molecular Plant Pathology, 2000. 57(3): p. 101-110. 99. Ramos, S., Effects of dietary flavonoids on apoptotic pathways related to cancer chemoprevention. The Journal of Nutritional Biochemistry, 2007. 18(7): p. 427-442. 100. Spencer, J.P.E., et al., Biomarkers of the intake of dietary polyphenols: strengths, limitations and application in nutrition research. British Journal of Nutrition, 2008. 99(1): p. 12-22. 101. Hu, M., Commentary: bioavailability of flavonoids and polyphenols: call to arms. Molecular pharmaceutics, 2007. 4(6): p. 803-806. 102. Akimoto, N., et al., FlavonoidSearch: A system for comprehensive flavonoid annotation by mass spectrometry. Scientific Reports, 2017. 7(1): p. 1243. 103. de Groot, H. and U. Rauen, Tissue injury by reactive oxygen species and the protective effects of flavonoids. Fundamental & Clinical Pharmacology, 1998. 12(3): p. 249-255. 104. Zhang, S., et al., Structure activity relationships and quantitative structure activity relationships for the flavonoid-mediated inhibition of breast cancer resistance protein. Biochemical Pharmacology, 2005. 70(4): p. 627-639. 105. Beecher, G.R., Overview of Dietary Flavonoids: Nomenclature, Occurrence and Intake. The Journal of Nutrition, 2003. 133(10): p. 3248S-3254S. 106. Goleniowski, M., et al., Phenolic Acids. 2013. p. 1951-1973. 107. Chong, J., A. Poutaraud, and P. Hugueney, Metabolism and roles of stilbenes in plants. Plant Science, 2009. 177(3): p. 143-155. 108. Moss, G.P., Nomenclature of Lignans and Neolignans (IUPAC Recommendations 2000), in Pure and Applied Chemistry. 2000. p. 1493. 109. Arts, I.C. and P.C. Hollman, Polyphenols and disease risk in epidemiologic studies. The American journal of clinical nutrition, 2005. 81(1): p. 317S-325S. 110. Clifford, M.N., Chlorogenic acids and other cinnamates–nature, occurrence, dietary burden, absorption and metabolism. Journal of the Science of Food and Agriculture, 2000. 80(7): p. 1033-1043. 111. Scalbert, A., et al., Dietary polyphenols and the prevention of diseases. Critical reviews in food science and nutrition, 2005. 45(4): p. 287-306. 112. Pandey, K.B., N. Mishra, and S.I. Rizvi, Protective role of myricetin on markers of oxidative stress in human erythrocytes subjected to oxidative stress. Natural product communications, 2009. 4(2): p. 1934578X0900400211. 113. Pandey, K.B. and S.I. Rizvi, Protective effect of resveratrol on markers of oxidative stress in human erythrocytes subjected to in vitro oxidative insult. Phytotherapy Research, 2010. 24(S1): p. S11-S14. 114. Aviram, M., et al., Pomegranate juice consumption reduces oxidative stress, atherogenic modifications to LDL, and platelet aggregation: studies in humans and in atherosclerotic apolipoprotein E–deficient mice. The American journal of clinical nutrition, 2000. 71(5): p. 1062-1076. 115. García-Lafuente, A., et al., Flavonoids as anti-inflammatory agents: implications in cancer and cardiovascular disease. Inflammation Research, 2009. 58(9): p. 537-552. 116. Yang, C.S., et al., Inhibition of carcinogenesis by dietary polyphenolic compounds. Annual review of nutrition, 2001. 21(1): p. 381-406. 117. Khan, N. and H. Mukhtar, Multitargeted therapy of cancer by green tea polyphenols. Cancer letters, 2008. 269(2): p. 269-280. 118. Rizvi, S.I., et al., Protective role of tea catechins against oxidation‐induced damage of type 2 diabetic erythrocytes. Clinical and Experimental Pharmacology and Physiology, 2005. 32(1‐2): p. 70-75. 119. Rizvi, S. and M.A. Zaid, Intracellular reduced glutathione content in normal and type 2 diabetic erythrocytes: effect of insulin and (-) epicatechin. Journal of Physiology and Pharmacology, 2001. 52(3). 120. Joseph, J.A., B. Shukitt-Hale, and G. Casadesus, Reversing the deleterious effects of aging on neuronal communication and behavior: beneficial properties of fruit polyphenolic compounds. The American Journal of Clinical Nutrition, 2005. 81(1): p. 313S-316S. 121. Rizvi, S.I. and P.K. Maurya, Alterations in antioxidant enzymes during aging in humans. Molecular Biotechnology, 2007. 37(1): p. 58-61. 122. Singh, M., et al., Challenges for research on polyphenols from foods in Alzheimer’s disease: bioavailability, metabolism, and cellular and molecular mechanisms. Journal of agricultural and food chemistry, 2008. 56(13): p. 4855-4873. 123. Aquilano, K., et al., Role of nitric oxide synthases in Parkinson’s disease: a review on the antioxidant and anti-inflammatory activity of polyphenols. Neurochemical research, 2008. 33(12): p. 2416-2426. 124. Zhang, J., et al., Polyphenolic extract from Rosa rugosa tea inhibits bacterial quorum sensing and biofilm formation. Food Control, 2014. 42: p. 125-131. 125. Choi, O., et al., Inhibitory effects of various plant polyphenols on the toxicity of Staphylococcal α-toxin. Microbial pathogenesis, 2007. 42(5-6): p. 215-224. 126. Daglia, M., Polyphenols as antimicrobial agents. Current opinion in biotechnology, 2012. 23(2): p. 174-181. 127. Chan, M.M.-Y., Antimicrobial effect of resveratrol on dermatophytes and bacterial pathogens of the skin. Biochemical Pharmacology, 2002. 63(2): p. 99-104. 128. Kumar, S. and A.K. Pandey, Chemistry and Biological Activities of Flavonoids: An Overview. The Scientific World Journal, 2013. 2013: p. 16. 129. Brown, L., et al., Through the wall: extracellular vesicles in Gram-positive bacteria, mycobacteria and fungi. Nature Reviews Microbiology, 2015. 13: p. 620. 130. Papuc, C., et al., Plant Polyphenols as Antioxidant and Antibacterial Agents for Shelf-Life Extension of Meat and Meat Products: Classification, Structures, Sources, and Action Mechanisms. Comprehensive Reviews in Food Science and Food Safety, 2017. 16(6): p. 1243-1268. 131. Sahoo, N., et al., Lysozyme in livestock: a guide to selection for disease resistance: a review. J. Anim. Sci. Adv, 2012. 2(4): p. 347-360. 132. Bilej, M., Chapter 9 - Mucosal Immunity in Invertebrates, in Mucosal Immunology (Fourth Edition), J. Mestecky, et al., Editors. 2015, Academic Press: Boston. p. 135-144. 133. Salton, M., The properties of lysozyme and its action on microorganisms. Bacteriological reviews, 1957. 21(2): p. 82. 134. Ibrahim, H., T. Matsuzaki, and T. Aoki, Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. Vol. 506. 2001. 27-32. 135. Bouaziz, Z., et al., Structure and antibacterial activity relationships of native and amyloid fibril lysozyme loaded on layered double hydroxide. Colloids and Surfaces B: Biointerfaces, 2017. 157: p. 10-17. 136. Wang, L., et al., Bacterial growth, detachment and cell size control on polyethylene terephthalate surfaces. Scientific Reports, 2015. 5: p. 15159. 137. Krebs, M.R.H., E.H.C. Bromley, and A.M. Donald, The binding of thioflavin-T to amyloid fibrils: localisation and implications. Journal of Structural Biology, 2005. 149(1): p. 30-37. 138. LeVine, H., [18] Quantification of β-sheet amyloid fibril structures with thioflavin T, in Methods in Enzymology. 1999, Academic Press. p. 274-284. 139. Levine III, H., Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Science, 1993. 2(3): p. 404-410. 140. Ray, S.S., S.K. Singh, and P. Balaram, An electrospray ionization mass spectrometry investigation of 1-anilino-8-naphthalene-sulfonate (ANS) binding to proteins. Journal of the American Society for Mass Spectrometry, 2001. 12(4): p. 428-438. 141. Hawe, A., M. Sutter, and W. Jiskoot, Extrinsic Fluorescent Dyes as Tools for Protein Characterization. Pharmaceutical Research, 2008. 25(7): p. 1487-1499. 142. Macosko, C.W., Rheology: principles, measurements, and applications. 143. Lucas-Abellán, C., et al., Resveratrol and cyclodextrins: Recent advances in encapsulation. 2013. p. 491-507. 144. Kitagawa, S., et al., Structure–Activity Relationships of the Inhibitory Effects of Flavonoids on P-Glycoprotein-Mediated Transport in KB-C2 Cells. Biological and Pharmaceutical Bulletin, 2005. 28(12): p. 2274-2278. 145. Brown, J.L., et al., Acid habituation of Escherichia coli and the potential role of cyclopropane fatty acids in low pH tolerance. International Journal of Food Microbiology, 1997. 37(2): p. 163-173. 146. Yao, Y., et al., Preformulation studies of myricetin: A natural antioxidant flavonoid. Vol. 69. 2014. 19-26. 147. Zupančič, Š., Z. Lavrič, and J. Kristl, Stability and solubility of trans-resveratrol are strongly influenced by pH and temperature. European Journal of Pharmaceutics and Biopharmaceutics, 2015. 93: p. 196-204. 148. Wadhwani, T., et al., Effect of various solvents on bacterial growth in context of determining MIC of various antimicrobials. Internet J. Microbiol, 2009. 7(1): p. 1-8. 149. Parekh, J., et al., Synthesis and antibacterial activity of some Schiff bases derived from 4-aminobenzoic acid. JOURNAL-SERBIAN CHEMICAL SOCIETY, 2005. 70(10): p. 1155. 150. Shariatizi, S., et al., Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols. International journal of biological macromolecules, 2015. 80: p. 95-106. 151. He, J., et al., Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme. Journal of Agricultural and Food Chemistry, 2014. 62(39): p. 9442-9449. 152. Cao, N., et al., Quinopeptide formation associated with the disruptive effect of epigallocatechin-gallate on lysozyme fibrils. International Journal of Biological Macromolecules, 2015. 78: p. 389-395. 153. Chen, R., et al., Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins. Archives of biochemistry and biophysics, 2011. 507(2): p. 343-349. 154. Hu, B., et al., Polyphenol-Binding Amyloid Fibrils Self-Assemble into Reversible Hydrogels with Antibacterial Activity. ACS Nano, 2018. 12(4): p. 3385-3396. 155. Kumar, D.K.V., et al., Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer’s disease. Science translational medicine, 2016. 8(340): p. 340ra72-340ra72. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/21712 | - |
dc.description.abstract | 本研究嘗試使用類澱粉纖維(amyloid fibril)結合多酚類(polyphenols),製作出具有抗菌性的水凝膠。本研究中的類澱粉纖維是以蛋白質本身即具有抗菌性的母雞蛋白溶菌酶製備而成,試圖強化所製得水凝膠之抗菌能力。多酚類則是選用了兩種亞類:黃酮類的楊梅素(myricetin)以及芪類的白藜蘆醇(resveratrol)。以上述原料製備了不同 pH 值以及不同的濃度的多酚類所製成之水凝膠,並比較了這些水凝膠的抗菌能力、外觀以及流體性質,此外還評估了不同濃度以及 pH 值環境下,此兩種多酚類對於類澱粉纖維的影響。
研究結果發現類澱粉纖維在加入多酚類之後,可以在接近中性的 pH 6 以及 pH 7.4 形成水凝膠;而在 pH 2 以及 pH 9 下則無法形成。 以革蘭氏陰性細菌 E. coli 進行抗菌測試,將樣品與菌液混合後於不同時間點取樣塗盤。實驗結果可以發現以楊梅素混合類澱粉纖維所製成的水凝膠具有良好的抗菌能力,在高濃度細菌環境下可在 8 小時內完全殺滅細菌;而以白藜蘆醇所製成之水凝膠以及單獨類澱粉纖維則不具有抗菌能力。 流變儀實驗結果可以觀察出水凝膠的黏度與 pH 值以及多酚類的濃度均有相關,且發現類澱粉纖維在加入多酚類後,黏度均有上升。然而隨著楊梅素加入的量越多,黏度的提升卻越少,是由於類澱粉纖維可能會被楊梅素所降解,造成其結構不穩定;而白藜蘆醇組別則無此現象。 從 ThT 螢光光譜分析可以發現,兩種多酚類對於類澱粉纖維的影響有巨大差異,楊梅素展現了很強的競爭 ThT 鍵結位置或是降解類澱粉纖維的能力,在高楊梅素濃度組別螢光強度比起單獨類澱粉纖維降低非常多,而白藜蘆醇則沒有很明 顯降低趨勢。 ANS 螢光光譜分析也可以觀察到加入楊梅素的組別螢光強度有急劇降低的趨勢,代表類澱粉纖維裸露的疏水區幾乎完全被楊梅素所佔據,或是楊梅素降解了類澱粉纖維結構。而白藜蘆醇的組別則同 ThT 結果沒有明顯變化。 綜上所述,在適當濃度下的楊梅素混和溶菌酶類澱粉纖維所製成的水凝膠,相較於單獨類澱粉纖維以及白藜蘆醇組別,具有更好的抗菌能力,且機械性質也較好,因此這種功能性水凝膠具有潛力成為抗菌生物材料。 | zh_TW |
dc.description.abstract | In this study, we attempted to produce antimicrobial composite hydrogels consisting of amyloid fibrils and polyphenolic molecules. The amyloid fibrils were made from hen egg-white lysozyme (HEWL), and myricetin and resveratrol were chosen as the polyphenolic molecules. The antibacterial capability, morphology and fluid property of the hydrogels prepared under different conditions were analyzed. The effects of these two polyphenols on amyloid fibrils were also evaluated.
Our results showed that, as opposed to the conditions at pH 2 and pH 9, HEWL amyloid fibrils were able to form hydrogels at pH 6 and pH 7.4 after the addition of polyphenols. The antibacterial activity assay was carried out with a high concentration of Gram-negative bacteria E. coli which was mixed with the hydrogel. The mixture was sampled at different times using the spread-plate method to observe for the colony formation. We found that the hydrogels incorporated with myricetin possessed a better antibacterial activity and eliminated bacteria within 8 hr. On the contrary, the amyloid fibril-based hydrogels with resveratrol and amyloid fibrils alone displayed negligible antibacterial activity. The results from the rheological analysis indicated that the viscosity of hydrogels is correlated with the pH value, concentration of polyphenol, and types of polyphenol. Moreover, it was found that the viscosity of the amyloid fibrils increased upon the addition of polyphenols. However, the more the amount of myricetin was added, the less the increase in viscosity. which might be attributed to the fact that the amyloid fibrils may be degraded by myricetin, resulting in structural instability. It should be noted that the similar trend was not seen in the groups with resveratrol. It could be found from the ThT binding analysis that the effects of myricetin and resveratrol on amyloid fibrils were significantly different. The myricetin molecule exhibited a strong competition with ThT for binding positions or ability to degrade amyloid fibrils. Therefore, in the groups of high concentrations of myricetin, the fluorescence intensity was observed to be much lower than that of amyloid fibrils alone. An analogous situation was also encountered in ANS binding analysis- showing that the occupation of exposed hydrophobic area of amyloid fibrillar structure by myricetin likely contributed to the reduction of ANS fluorescence intensity. However, this drastic reduction in ANS fluorescence emission was not perceived in the hydrogels combined with resveratrol. Moreover, hydrogels with the molar ratio of lysozyme fibril to myricetin at 0.1:1 showed better antibacterial ability and mechanical property. Therefore, this hydrogel is a promising antibacterial composite material. The outcome from this study is in support of the potential application of amyloid fibrils as functional biomaterials. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T03:43:36Z (GMT). No. of bitstreams: 1 ntu-108-R06524090-1.pdf: 54086807 bytes, checksum: ce5270c010ba860c77615c05816a3c0d (MD5) Previous issue date: 2019 | en |
dc.description.tableofcontents | 誌謝 I
中文摘要 II Abstract IV 目 錄 VI 圖目錄 IX 表目錄 XII 第一章 緒論 1 1-1. 研究動機 1 第二章 文獻回顧 3 2-1. 蛋白質與蛋白質結構 3 2-1-1. 蛋白質 3 2-1-2. 胺基酸 4 2-1-3. 一級~四級結構 5 2-1-4. 蛋白質摺疊與聚集 8 2-2. 類澱粉纖維 9 2-2-1. 類澱粉纖維的致病性 10 2-2-2. 類澱粉纖維結構 11 2-3. 蛋白質與類澱粉纖維於應用材料之潛力 12 2-3-1. 食物蛋白質類澱粉纖維於食品加工之應用潛力 12 2-3-2. 生物感測器(Biosensors) 14 2-3-3. 生物吸附劑(Bioabsorbent) 18 2-3-4. 水凝膠(Hydrogels) 19 2-3-5. 微膠囊(Microcapsules) 30 2-3-6. Fibrillosomes 32 2-4. 多酚類(Polyphenols) 35 2-4-1. 多酚類種類、結構以及來源簡介 35 2-4-2. 多酚類的抗氧化性、抗菌性以及保健作用 42 2-4-3. 多酚類的抗菌機制 44 2-5. 多酚類結合溶菌酶類澱粉纖維形成具有抗菌性的水凝膠 45 2-5-1. 溶菌酶 45 2-6. 實驗原理介紹 48 2-6-1. 微生物培養 48 2-6-2. 細菌培養以及劃盤法 48 2-6-3. ThT(Thioflavin T)螢光染色法 49 2-6-4. ANS(1-anilino-8-naphthalene sulfonate)螢光染色法 50 2-6-5. 旋轉流變儀(Rheometer) 51 第三章 實驗方法 52 3-1. 實驗菌株 52 3-2. 實驗儀器與藥品 52 3-3. 實驗方法與步驟 55 3-3-1. 母雞蛋白溶菌酶類澱粉纖維製備 55 3-3-2. Bis-Tris緩衝溶液(Bis-Tris buffer)製備 55 3-3-3. 多酚類儲備溶液(polyphenol stock solution)製備 55 3-3-4. 多酚類結合類澱粉纖維之水凝膠製備 56 3-3-5. 對照組製備 57 3-3-6. 固態培養基與液態培養基製備 58 3-3-7. 細菌培養以及定量 58 3-3-8. 水凝膠抑菌實驗 60 3-3-9. ThT螢光光譜分析 60 3-3-10. ANS螢光光譜分析 61 3-3-11. 流變儀(Rheometer) 62 第四章 實驗結果與討論 63 4-1. 水凝膠型態以及外觀觀察結果 63 4-2. 多酚類濃度以及pH環境對於水凝膠抗菌活性之影響。 66 4-3. 流變儀實驗結果討論 70 4-4. ThT與ANS螢光光譜分析實驗結果 74 4-5. 針對楊梅素水凝膠中的各成分之抗菌活性進行比較 80 4-6. 與文獻比較 84 第五章 結論與未來展望 88 參考文獻 90 附錄 103 | |
dc.language.iso | zh-TW | |
dc.title | 類澱粉纖維複合生物材料之應用:製備具有抗菌功能之與多酚分子結合的類澱粉纖維水凝膠複合材料 | zh_TW |
dc.title | Applications of Amyloid Fibril-Based Hybrid Biomaterials: Preparation of Antibacterial Composite Hydrogels Consisting of Amyloid Fibrils and Polyphenolic Molecules | en |
dc.type | Thesis | |
dc.date.schoolyear | 107-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 林達顯,侯劭毅,賴進此,吳宛儒 | |
dc.subject.keyword | 溶菌?,類澱粉纖維,多酚類,抗菌活性,水凝膠, | zh_TW |
dc.subject.keyword | lysozyme,amyloid fibrils,polyphenols,antimicrobial activity,hydrogel, | en |
dc.relation.page | 106 | |
dc.identifier.doi | 10.6342/NTU201900760 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2019-06-05 | |
dc.contributor.author-college | 工學院 | zh_TW |
dc.contributor.author-dept | 化學工程學研究所 | zh_TW |
顯示於系所單位: | 化學工程學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-108-1.pdf 目前未授權公開取用 | 52.82 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。