References
Anand U, Jash C, Mukherjee S. 2011.
Protein unfolding and subsequent refolding: a spectroscopic
investigation. Physical Chemistry Chemical Physics 13(45):20418-20426.
Anema SG, McKenna AB. 1996. Reaction
kinetics of thermal denaturation of whey proteins in heated
reconstituted whole milk. Journal of Agricultural and Food Chemistry
44(2):422-428.
Arakawa T, Kita Y. 2000. Protection of
bovine serum albumin from aggregation by Tween 80. Journal of
pharmaceutical sciences 89(5):646-651.
Barnes HA, Hutton JF, Walters K. 1989.
An introduction to rheology: Elsevier.
Bekard IB, Asimakis P, Teoh CL, Ryan
T, Howlett GJ, Bertolini J, Dunstan DE. 2012. Bovine serum albumin
unfolds in Couette flow. Soft Matter 8(2):385-389.
Belitz H-D, Grosch W. 2013. Lehrbuch
der lebensmittelchemie: Springer-Verlag.
Bogahawaththa D, Vasiljevic T. 2020.
Shearing accelerates denaturation of β-lactoglobulin and α-lactalbumin
in skim milk during heating. International Dairy Journal 105:104674.
Bratko D, Cellmer T, Prausnitz JM,
Blanch HW. 2007. Molecular simulation of protein aggregation.
Biotechnology and bioengineering 96(1):1-8.
Chen M, Liu Y, Cao H, Song L, Zhang Q.
2015. The secondary and aggregation structural changes of BSA induced by
trivalent chromium: A biophysical study. Journal of Luminescence
158:116-124.
Chiti F, Dobson CM. 2017. Protein
misfolding, amyloid formation, and human disease: a summary of progress
over the last decade. Annual review of biochemistry 86:27-68.
Collins SR, Douglass A, Vale RD,
Weissman JS. 2004. Mechanism of prion propagation: amyloid growth occurs
by monomer addition. PLoS Biol 2(10):e321.
Danielsson J, Mu X, Lang L, Wang H,
Binolfi A, Theillet F-X, Bekei B, Logan DT, Selenko P, Wennerström H.
2015. Thermodynamics of protein destabilization in live cells.
Proceedings of the National Academy of Sciences 112(40):12402-12407.
Dobson J, Kumar A, Willis LF, Tuma R,
Higazi DR, Turner R, Lowe DC, Ashcroft AE, Radford SE, Kapur N. 2017.
Inducing protein aggregation by extensional flow. Proceedings of the
National Academy of Sciences 114(18):4673-4678.
Dubey K, Anand BG, Shekhawat DS, Kar
K. 2017. Eugenol prevents amyloid formation of proteins and inhibits
amyloid-induced hemolysis. Scientific reports 7:40744.
Elofsson C, Dejmek P, Paulsson M,
Burling H. 1997. Atomic force microscopy studies on whey proteins.
International dairy journal 7(12):813-819.
Greenfield NJ. 2006. Using circular
dichroism collected as a function of temperature to determine the
thermodynamics of protein unfolding and binding interactions. Nature
protocols 1(6):2527.
Grigolato F, Arosio P. 2019.
Synergistic effects of flow and interfaces on antibody aggregation.
Biotechnology and bioengineering.
Haynes CA, Norde W. 1995. Structures
and stabilities of adsorbed proteins. Journal of colloid and interface
science 169(2):313-328.
Hill EK, Krebs B, Goodall DG, Howlett
GJ, Dunstan DE. 2006. Shear flow induces amyloid fibril formation.
Biomacromolecules 7(1):10-13.
Holm NK, Jespersen SK, Thomassen LV,
Wolff TY, Sehgal P, Thomsen LA, Christiansen G, Andersen CB, Knudsen AD,
Otzen DE. 2007. Aggregation and fibrillation of bovine serum albumin.
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics
1774(9):1128-1138.
Iannazzo D, Pistone A, Ziccarelli I,
Galvagno S. 2018. Graphene-based materials for application in
pharmaceutical nanotechnology. Fullerens, Graphenes and Nanotubes:
Elsevier. p 297-329.
Ismael MA, Khan JM, Malik A,
Alsenaidy MA, Hidayathulla S, Khan RH, Sen P, Irfan M, Alsenaidy AM.
2018. Unraveling the molecular mechanism of the effects of sodium
dodecyl sulfate, salts, and sugars on amyloid fibril formation in camel
IgG. Colloids and Surfaces B: Biointerfaces 170:430-437.
Jayamani J, Shanmugam G. 2017.
Diameter of the vial plays a crucial role in the amyloid fibril
formation: Role of interface area between hydrophilic-hydrophobic
surfaces. International journal of biological macromolecules
101:290-298.
Johnson Jr WC. 1988. Secondary
structure of proteins through circular dichroism spectroscopy. Annual
review of biophysics and biophysical chemistry 17(1):145-166.
Kamada A, Mittal N, Söderberg LD,
Ingverud T, Ohm W, Roth SV, Lundell F, Lendel C. 2017. Flow-assisted
assembly of nanostructured protein microfibers. Proceedings of the
National Academy of Sciences 114(6):1232-1237.
Khurana R, Coleman C, Ionescu-Zanetti
C, Carter SA, Krishna V, Grover RK, Roy R, Singh S. 2005. Mechanism of
thioflavin T binding to amyloid fibrils. Journal of structural biology
151(3):229-238.
Kong J-Y, Miyawaki O, Nakamura K,
Yano T. 1982. The “intrinsic” thermal conductivity of some wet
proteins in relation to their average hydrophobicity: analyses on gels
of egg-albumin, wheat gluten and milk casein. Agricultural and
Biological Chemistry 46(3):789-794.
Lansbury PT, Lashuel HA. 2006. A
century-old debate on protein aggregation and neurodegeneration enters
the clinic. Nature 443(7113):774-779.
Liu J-J, Lindquist S. 1999.
Oligopeptide-repeat expansions modulate ‘protein-only’inheritance in
yeast. Nature 400(6744):573-576.
Manoi K, Rizvi SS. 2008. Rheological
characterizations of texturized whey protein concentrate-based powders
produced by reactive supercritical fluid extrusion. Food Research
International 41(8):786-796.
Maruyama T, Katoh S, Nakajima M,
Nabetani H. 2001. Mechanism of bovine serum albumin aggregation during
ultrafiltration. Biotechnology and bioengineering 75(2):233-238.
Militello V, Vetri V, Leone M. 2003.
Conformational changes involved in thermal aggregation processes of
bovine serum albumin. Biophysical chemistry 105(1):133-141.
Murayama K, Tomida M. 2004.
Heat-induced secondary structure and conformation change of bovine serum
albumin investigated by Fourier transform infrared spectroscopy.
Biochemistry 43(36):11526-11532.
Nelson DL, Cox MM, Lehninger AL.
2008. Principles of biochemistry: Freeman New York:.
Pal S, Pyne P, Samanta N, Ebbinghaus
S, Mitra RK. 2020. Thermal stability modulation of the native and
chemically-unfolded state of bovine serum albumin by amino acids.
Physical Chemistry Chemical Physics 22(1):179-188.
Pandey LM, Le Denmat S, Delabouglise
D, Bruckert F, Pattanayek SK, Weidenhaupt M. 2012. Surface chemistry at
the nanometer scale influences insulin aggregation. Colloids and
Surfaces B: Biointerfaces 100:69-76.
Pandey LM, Pattanayek SK,
Delabouglise D. 2013. Properties of adsorbed bovine serum albumin and
fibrinogen on self-assembled monolayers. The Journal of Physical
Chemistry C 117(12):6151-6160.
Paul BK, Ray D, Guchhait N. 2013.
Unraveling the binding interaction and kinetics of a prospective
anti-HIV drug with a model transport protein: results and challenges.
Physical Chemistry Chemical Physics 15(4):1275-1287.
Quevedo M, Kulozik U, Karbstein HP,
Emin MA. 2020. Kinetics of denaturation and aggregation of highly
concentrated β-Lactoglobulin under defined thermomechanical treatment.
Journal of Food Engineering 274:109825.
Rondeau P, Navarra G, Cacciabaudo F,
Leone M, Bourdon E, Militello V. 2010. Thermal aggregation of glycated
bovine serum albumin. Biochimica et Biophysica Acta (BBA)-Proteins and
Proteomics 1804(4):789-798.
Ross CA, Poirier MA. 2004. Protein
aggregation and neurodegenerative disease. Nature medicine
10(7):S10-S17.
Serio TR, Cashikar AG, Kowal AS,
Sawicki GJ, Moslehi JJ, Serpell L, Arnsdorf MF, Lindquist SL. 2000.
Nucleated conformational conversion and the replication of
conformational information by a prion determinant. Science
289(5483):1317-1321.
Sheu S-Y, Yang D-Y, Selzle H, Schlag
E. 2003. Energetics of hydrogen bonds in peptides. Proceedings of the
National Academy of Sciences 100(22):12683-12687.
Singh A, Datta P, Pandey LM. 2017.
Deciphering the mechanistic insight into the stoichiometric ratio
dependent behavior of Cu (II) on BSA fibrillation. International journal
of biological macromolecules 97:662-670.
Smith JM. 1950. Introduction to
chemical engineering thermodynamics. ACS Publications.
Solá RJ, Al‐Azzam W, Griebenow K.
2006. Engineering of protein thermodynamic, kinetic, and colloidal
stability: Chemical glycosylation with monofunctionally activated
glycans. Biotechnology and bioengineering 94(6):1072-1079.
Sprague-Piercy MA, Wong E, Roskamp
KW, Fakhoury JN, Freites JA, Tobias DJ, Martin RW. 2020. Human
αB-crystallin discriminates between aggregation-prone and
function-preserving variants of a client protein. Biochimica et
Biophysica Acta (BBA)-General Subjects 1864(3):129502.
Vetri V, Librizzi F, Leone M,
Militello V. 2007. Thermal aggregation of bovine serum albumin at
different pH: comparison with human serum albumin. European Biophysics
Journal 36(7):717-725.
Wälchli R, Ressurreição M, Vogg S,
Feidl F, Angelo J, Xu X, Ghose S, Jian Li Z, Le Saoût X, Souquet J.
2020. Understanding mAb aggregation during low pH viral inactivation and
subsequent neutralization. Biotechnology and Bioengineering
117(3):687-700.
Wolfe LS, Calabrese MF, Nath A, Blaho
DV, Miranker AD, Xiong Y. 2010. Protein-induced photophysical changes to
the amyloid indicator dye thioflavin T. Proceedings of the National
Academy of Sciences 107(39):16863-16868.
Yamasaki M, Yano H, Aoki K. 1990.
Differential scanning calorimetric studies on bovine serum albumin: I.
Effects of pH and ionic strength. International journal of biological
macromolecules 12(4):263-268.