Gregory RB (1995) Protein-solvent interactions. Marcel Dekker, Inc New York 445–479

Gekko K, Timasheff SN (1981) Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20:4667–4676. https://doi.org/10.1021/bi00519a023

Article  CAS  PubMed  Google Scholar 

Usha R, Ramasami T (2008) Stability of collagen with polyols against guanidine denaturation. Coll Surfaces B Biointerfaces 61:39–42. https://doi.org/10.1016/j.colsurfb.2007.07.005

Article  CAS  Google Scholar 

Yu Y, Wang J, Shao Q et al (2016) The effects of organic solvents on the folding pathway and associated thermodynamics of proteins: a microscopic view. Sci Rep 6:1–12. https://doi.org/10.1038/srep19500

Article  CAS  Google Scholar 

Davis-Searles PR, Saunders AJ, Erie DA et al (2001) Interpreting the effects of small uncharged solutes on protein-folding equilibria. Annu Rev Biophys Biomol Struct 30:271–306. https://doi.org/10.1146/annurev.biophys.30.1.271

Article  CAS  PubMed  Google Scholar 

Upadhyay A, Chhangani D, Rao NR et al (2023) Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity. Mol Neurodegener 18:1–22

Article  Google Scholar 

Lumpkin CJ, Patel H, Potts GK et al (2024) Broad proteomics analysis of seeding-induced aggregation of α-synuclein in M83 neurons reveals remodeling of proteostasis mechanisms that might contribute to Parkinson’s disease pathogenesis. Mol Brain 17:1–16

Article  Google Scholar 

Mondal B, Reddy G (2019) Cosolvent effects on the growth of protein aggregates formed by a single domain globular protein and an intrinsically disordered protein. J Phys Chem B 123:1950–1960

Article  CAS  PubMed  Google Scholar 

Reddy G, Muttathukattil AN, Mondal B (2020) Cosolvent effects on the growth of amyloid fibrils. Curr Opin Struct Biol 60:101–109. https://doi.org/10.1016/J.SBI.2019.12.011

Article  CAS  PubMed  Google Scholar 

Lee JC, Timasheff SN (1981) The stabilization of proteins by sucrose. J Biol Chem 256:7193–7201. https://doi.org/10.1016/S0021-9258(19)68947-7

Article  CAS  PubMed  Google Scholar 

Pittz EP, Timasheff SN (1978) Interaction of ribonuclease a with aqueous 2-methyl-2,4-pentanediol at pH 5.8. Biochemistry 17:615–623. https://doi.org/10.1021/bi00597a009

Article  CAS  PubMed  Google Scholar 

Oprzeska-Zingrebe EA, Smiatek J (2018) Preferential binding of urea to single-stranded DNA structures: a molecular dynamics study. Biophys J 114:1551–1562. https://doi.org/10.1016/j.bpj.2018.02.013

Article  CAS  PubMed  PubMed Central  Google Scholar 

Gekko K, Ohmae E, Kameyama K, Takagi T (1998) Acetonitrile-protein interactions: amino acid solubility and preferential solvation. Biochim Biophys Acta - Protein Struct Mol Enzymol 1387:195–205. https://doi.org/10.1016/S0167-4838(98)00121-6

Article  CAS  Google Scholar 

Arakawa T, Kita Y, Timasheff SN (2007) Protein precipitation and denaturation by dimethyl sulfoxide. Biophys Chem 131:62–70. https://doi.org/10.1016/J.BPC.2007.09.004

Article  CAS  PubMed  Google Scholar 

Shimizu S, Smith DJ (2004) Preferential hydration and the exclusion of cosolvents from protein surfaces. J Chem Phys 121:1148–1154. https://doi.org/10.1063/1.1759615

Article  CAS  PubMed  Google Scholar 

Schummel PH, Jaworek MW, Rosin C et al (2018) Exploring the influence of natural cosolvents on the free energy and conformational landscape of filamentous actin and microtubules. Phys Chem Chem Phys 20:28400–28411. https://doi.org/10.1039/C8CP03041C

Article  CAS  PubMed  Google Scholar 

Canchi DR, García AE (2013) Cosolvent effects on protein stability. Annu Rev Phys Chem 64:273–293

Article  CAS  PubMed  Google Scholar 

Priya MH, Ashbaugh HS, Paulaitis ME (2011) Cosolvent preferential molecular interactions in aqueous solutions. J Phys Chem B 115:13633–13642

Article  CAS  PubMed  Google Scholar 

Shimizu S, Matubayasi N (2014) Preferential solvation: Dividing surface vs excess numbers. J Phys Chem B 118:3922–3930

Article  CAS  PubMed  Google Scholar 

Smith PE (1999) Computer simulation of cosolvent effects on hydrophobic hydration. J Phys Chem B 103:525–534. https://doi.org/10.1021/jp983303c

Article  CAS  Google Scholar 

Chitra R, Smith PE (2001) Preferential interactions of cosolvents with hydrophobic solutes. J Phys Chem B 105:11513–11522. https://doi.org/10.1021/jp012354y

Article  CAS  Google Scholar 

Aburi M, Smith PE (2004) A combined simulation and Kirkwood-Buff approach to quantify cosolvent effects on the conformational preferences of peptides in solution. J Phys Chem B 108:7382–7388. https://doi.org/10.1021/jp036582z

Article  CAS  Google Scholar 

Shimizu S, Boon CL (2004) The Kirkwood-Buff theory and the effect of cosolvents on biochemical reactions. J Chem Phys 121:9147–9155. https://doi.org/10.1063/1.1806402

Article  CAS  PubMed  Google Scholar 

Davis L, Chin JW (2012) Designer proteins: applications of genetic code expansion in cell biology. Nat Rev Mol Cell Biol 13:168–182. https://doi.org/10.1038/nrm3286

Article  CAS  PubMed  Google Scholar 

Parsegian VA, Rand RP, Rau DC (2000) Osmotic stress, crowding, preferential hydration, and binding: a comparison of perspectives. Proc Natl Acad Sci 97:3987–3992. https://doi.org/10.1073/PNAS.97.8.3987

Article  CAS  PubMed  PubMed Central  Google Scholar 

Shimizu S, Matubayasi N (2018) A unified perspective on preferential solvation and adsorption based on inhomogeneous solvation theory. Phys A Stat Mech its Appl 492:1988–1996. https://doi.org/10.1016/J.PHYSA.2017.11.113

Article  CAS  Google Scholar 

Baynes BM, Trout BL (2003) Proteins in mixed solvents: A molecular-level perspective. J Phys Chem B 107:14058–14067. https://doi.org/10.1021/jp0363996

Article  CAS  Google Scholar 

Timasheff SN (1993) The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu Rev Biophys Biomol Struct 22:67–97. https://doi.org/10.1146/annurev.bb.22.060193.000435

Article  CAS  PubMed  Google Scholar 

Shukla D, Shinde C, Trout BL (2009) Molecular computations of preferential interaction coefficients of proteins. J Phys Chem B 113:12546–12554

Article  CAS  PubMed  Google Scholar 

Oleinikova A, Brovchenko I, Singh G (2010) The temperature dependence of the heat capacity of hydration water near biosurfaces from molecular simulations. Europhys Lett 90:36001. https://doi.org/10.1209/0295-5075/90/36001

Article  CAS  Google Scholar 

Xie G, Timasheff SN (1997) The thermodynamic mechanism of protein stabilization by trehalose. Biophys Chem 64:25–43. https://doi.org/10.1016/S0301-4622(96)02222-3

Article  CAS  PubMed  Google Scholar 

Brovchenko I, Oleinikova A (2008) Which properties of a spanning network of hydration water enable biological functions? ChemPhysChem 9:2695–2702. https://doi.org/10.1002/CPHC.200800662

Article  CAS  PubMed