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Journal articles on the topic 'Hydrophobic interaction'

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Published: 4 June 2021
Last updated: 10 March 2023

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1

Roettger, Belinda F., and Michael R. Ladisch. "Hydrophobic interaction chromatography." Biotechnology Advances 7, no. 1 (1989): 15–29. http://dx.doi.org/10.1016/0734-9750(89)90901-4.

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2

Kårsnäs, Per, and Tua Lindblom. "Characterization of hydrophobic interaction and hydrophobic interaction chromatography media by multivariate analysis." Journal of Chromatography A 599, no. 1-2 (1992): 131–36. http://dx.doi.org/10.1016/0021-9673(92)85465-6.

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3

Ohno, Nobumichi, and Shintaro Sugai. "Isotope effects on hydrophobic interaction in hydrophobic polyelectrolytes." Macromolecules 18, no. 6 (1985): 1287–91. http://dx.doi.org/10.1021/ma00148a042.

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4

Yau, Tak-Yu, William Sander, Christian Eidson, and Albert J. Courey. "SUMO Interacting Motifs: Structure and Function." Cells 10, no. 11 (2021): 2825. http://dx.doi.org/10.3390/cells10112825.

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Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-related protein family. SUMO modulates protein function through covalent conjugation to lysine residues in a large number of proteins. Once covalently conjugated to a protein, SUMO often regulates that protein’s function by recruiting other cellular proteins. Recruitment frequently involves a non-covalent interaction between SUMO and a SUMO-interacting motif (SIM) in the interacting protein. SIMs generally consist of a four-residue-long hydrophobic stretch of amino acids with aliphatic non-polar side chains flanked on one side by negatively charged amino acid residues. The SIM assumes an extended β-strand-like conformation and binds to a conserved hydrophobic groove in SUMO. In addition to hydrophobic interactions between the SIM non-polar core and hydrophobic residues in the groove, the negatively charged residues in the SIM make favorable electrostatic contacts with positively charged residues in and around the groove. The SIM/SUMO interaction can be regulated by the phosphorylation of residues adjacent to the SIM hydrophobic core, which provide additional negative charges for favorable electrostatic interaction with SUMO. The SUMO interactome consists of hundreds or perhaps thousands of SIM-containing proteins, but we do not fully understand how each SUMOylated protein selects the set of SIM-containing proteins appropriate to its function. SIM/SUMO interactions have critical functions in a large number of essential cellular processes including the formation of membraneless organelles by liquid–liquid phase separation, epigenetic regulation of transcription through histone modification, DNA repair, and a variety of host–pathogen interactions.
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5

Gao, Dong, Fu-Chun Tan, Wen-Peng Wang, and Li-Li Wang. "Resolution enhancement in hydrophobic interaction chromatography via electrostatic interactions." Chinese Chemical Letters 24, no. 5 (2013): 419–21. http://dx.doi.org/10.1016/j.cclet.2013.03.004.

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6

Vu, Anh, Xianghong Qian, and S. Ranil Wickramasinghe. "Membrane-based hydrophobic interaction chromatography." Separation Science and Technology 52, no. 2 (2016): 287–98. http://dx.doi.org/10.1080/01496395.2016.1247865.

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7

Hahn, Rainer, Karin Deinhofer, Christine Machold, and Alois Jungbauer. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography B 790, no. 1-2 (2003): 99–114. http://dx.doi.org/10.1016/s1570-0232(03)00080-1.

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8

Jungbauer, Alois, Christine Machold, and Rainer Hahn. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography A 1079, no. 1-2 (2005): 221–28. http://dx.doi.org/10.1016/j.chroma.2005.04.002.

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9

Kolomeisky, A. B., and B. Widom. "Model of the hydrophobic interaction." Faraday Discussions 112 (1999): 81–89. http://dx.doi.org/10.1039/a809308c.

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10

Machold, Christine, Karin Deinhofer, Rainer Hahn, and Alois Jungbauer. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography A 972, no. 1 (2002): 3–19. http://dx.doi.org/10.1016/s0021-9673(02)01077-4.

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11

Queiroz, J. A., C. T. Tomaz, and J. M. S. Cabral. "Hydrophobic interaction chromatography of proteins." Journal of Biotechnology 87, no. 2 (2001): 143–59. http://dx.doi.org/10.1016/s0168-1656(01)00237-1.

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12

To, Brian C. S., and Abraham M. Lenhoff. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography A 1141, no. 2 (2007): 191–205. http://dx.doi.org/10.1016/j.chroma.2006.12.020.

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13

To, Brian C. S., and Abraham M. Lenhoff. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography A 1141, no. 2 (2007): 235–43. http://dx.doi.org/10.1016/j.chroma.2006.12.022.

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14

Ueberbacher, Rene, Emmerich Haimer, Rainer Hahn, and Alois Jungbauer. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography A 1198-1199 (July 2008): 154–63. http://dx.doi.org/10.1016/j.chroma.2008.05.062.

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15

To, Brian C. S., and Abraham M. Lenhoff. "Hydrophobic interaction chromatography of proteins." Journal of Chromatography A 1205, no. 1-2 (2008): 46–59. http://dx.doi.org/10.1016/j.chroma.2008.07.079.

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16

Weaver, David L. "Hydrophobic interaction between globin helices." Biopolymers 32, no. 5 (1992): 477–90. http://dx.doi.org/10.1002/bip.360320504.

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17

Diaz, T., L. Franco Fraguas, B. Luna, B. Brena, and F. Batista-Viera. "Hydrophobic interaction chromatography of amylases." Journal of High Resolution Chromatography 12, no. 8 (1989): 570–72. http://dx.doi.org/10.1002/jhrc.1240120823.

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18

Hara, Kodai, Masayuki Uchida, Risa Tagata, et al. "Structure of proliferating cell nuclear antigen (PCNA) bound to an APIM peptide reveals the universality of PCNA interaction." Acta Crystallographica Section F Structural Biology Communications 74, no. 4 (2018): 214–21. http://dx.doi.org/10.1107/s2053230x18003242.

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Proliferating cell nuclear antigen (PCNA) provides a molecular platform for numerous protein–protein interactions in DNA metabolism. A large number of proteins associated with PCNA have a well characterized sequence termed the PCNA-interacting protein box motif (PIPM). Another PCNA-interacting sequence termed the AlkB homologue 2 PCNA-interacting motif (APIM), comprising the five consensus residues (K/R)-(F/Y/W)-(L/I/V/A)-(L/I/V/A)-(K/R), has also been identified in various proteins. In contrast to that with PIPM, the PCNA–APIM interaction is less well understood. Here, the crystal structure of PCNA bound to a peptide carrying an APIM consensus sequence, RFLVK, was determined and structure-based interaction analysis was performed. The APIM peptide binds to the PIPM-binding pocket on PCNA in a similar way to PIPM. The phenylalanine and leucine residues within the APIM consensus sequence and a hydrophobic residue that precedes the APIM consensus sequence are crucially involved in interactions with the hydrophobic pocket of PCNA. This interaction is essential for overall binding. These results provide a structural basis for regulation of the PCNA interaction and might aid in the development of specific inhibitors of this interaction.
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19

Ahuja, Eric S., and Joe P. Foley. "Separation of very hydrophobic compounds by hydrophobic interaction electrokinetic chromatography." Journal of Chromatography A 680, no. 1 (1994): 73–83. http://dx.doi.org/10.1016/0021-9673(94)80054-5.

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20

Wang, Gang, Tobias Hahn, and Jürgen Hubbuch. "Water on hydrophobic surfaces: Mechanistic modeling of hydrophobic interaction chromatography." Journal of Chromatography A 1465 (September 2016): 71–78. http://dx.doi.org/10.1016/j.chroma.2016.07.085.

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21

Takeda, Takashi, Jun'ya Tsutsumi, Tatsuo Hasegawa, Shin-ichiro Noro, Takayoshi Nakamura, and Tomoyuki Akutagawa. "Electron-deficient acene-based liquid crystals: dialkoxydicyanopyrazinoquinoxalines." Journal of Materials Chemistry C 3, no. 13 (2015): 3016–22. http://dx.doi.org/10.1039/c5tc00022j.

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Dialkoxydicyanopyrazinoquinoxaline exhibited liquid crystallinity, which was cooperatively stabilized by three noncovalent interactions, i.e. hydrophobic interaction, dipole–dipole interaction and π–π interaction.
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22

Lu, Shouci. "Hydrophobic interaction in flocculation and flotation 3. Role of hydrophobic interaction in particle—bubble attachment." Colloids and Surfaces 57, no. 1 (1991): 73–81. http://dx.doi.org/10.1016/0166-6622(91)80181-m.

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23

Donaldson, Stephen H., Anja Røyne, Kai Kristiansen, et al. "Developing a General Interaction Potential for Hydrophobic and Hydrophilic Interactions." Langmuir 31, no. 7 (2014): 2051–64. http://dx.doi.org/10.1021/la502115g.

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24

Chen, Lihong, Wade Borcherds, Shaofang Wu, et al. "Autoinhibition of MDMX by intramolecular p53 mimicry." Proceedings of the National Academy of Sciences 112, no. 15 (2015): 4624–29. http://dx.doi.org/10.1073/pnas.1420833112.

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The p53 inhibitor MDMX is controlled by multiple stress signaling pathways. Using a proteolytic fragment release (PFR) assay, we detected an intramolecular interaction in MDMX that mechanistically mimics the interaction with p53, resulting in autoinhibition of MDMX. This mimicry is mediated by a hydrophobic peptide located in a long disordered central segment of MDMX that has sequence similarity to the p53 transactivation domain. NMR spectroscopy was used to show this hydrophobic peptide interacts with the N-terminal domain of MDMX in a structurally analogous manner to p53. Mutation of two critical tryptophan residues in the hydrophobic peptide disrupted the intramolecular interaction and increased p53 binding, providing further evidence for mechanistic mimicry. The PFR assay also revealed a second intramolecular interaction between the RING domain and central region that regulates MDMX nuclear import. These results establish the importance of intramolecular interactions in MDMX regulation, and validate a new assay for the study of intramolecular interactions in multidomain proteins with intrinsically disordered regions.
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25

Tanford, Charles. "Organizational consequences of the hydrophobic interaction." Proceedings / Indian Academy of Sciences 98, no. 5-6 (1987): 343–56. http://dx.doi.org/10.1007/bf02861533.

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26

Christenson, Hugo K., Per M. Claesson, and Richard M. Pashley. "The hydrophobic interaction between macroscopic surfaces." Proceedings / Indian Academy of Sciences 98, no. 5-6 (1987): 379–89. http://dx.doi.org/10.1007/bf02861535.

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27

Nakanishi, Koichiro, and Hideki Tanaka. "Molecular dynamics study on hydrophobic interaction." Bulletin of the Japan Institute of Metals 29, no. 6 (1990): 465–69. http://dx.doi.org/10.2320/materia1962.29.465.

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28

Luzar, A., D. Bratko, and L. Blum. "Monte Carlo simulation of hydrophobic interaction." Journal of Chemical Physics 86, no. 5 (1987): 2955–59. http://dx.doi.org/10.1063/1.452047.

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29

Wood, Jonathan, and Ravi Sharma. "Interaction forces between hydrophobic mica surfaces." Journal of Adhesion Science and Technology 9, no. 8 (1995): 1075–85. http://dx.doi.org/10.1163/156856195x00914.

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30

Belyaev, Aleksey V., and Olga I. Vinogradova. "Hydrodynamic interaction with super-hydrophobic surfaces." Soft Matter 6, no. 18 (2010): 4563. http://dx.doi.org/10.1039/c0sm00205d.

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31

Aerts, Tony, and Julius Clauwaert. "Thermodynamic parameters involved in hydrophobic interaction." Journal of Chemical Education 63, no. 11 (1986): 993. http://dx.doi.org/10.1021/ed063p993.

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32

Schellman, J. A. "Temperature, stability, and the hydrophobic interaction." Biophysical Journal 73, no. 6 (1997): 2960–64. http://dx.doi.org/10.1016/s0006-3495(97)78324-3.

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33

Vailaya, Anant, and Csaba Horváth. "Retention Thermodynamics in Hydrophobic Interaction Chromatography." Industrial & Engineering Chemistry Research 35, no. 9 (1996): 2964–81. http://dx.doi.org/10.1021/ie9507437.

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34

Himstedt, Heath H., Xianghong Qian, Justin R. Weaver, and S. Ranil Wickramasinghe. "Responsive membranes for hydrophobic interaction chromatography." Journal of Membrane Science 447 (November 2013): 335–44. http://dx.doi.org/10.1016/j.memsci.2013.07.020.

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35

Wetlaufer, D. B., and M. R. Koenigbauer. "Surfactant-mediated protein hydrophobic-interaction chromatography." Journal of Chromatography A 359 (January 1986): 55–60. http://dx.doi.org/10.1016/0021-9673(86)80061-9.

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36

Haimer, Emmerich, Anne Tscheliessnig, Rainer Hahn, and Alois Jungbauer. "Hydrophobic interaction chromatography of proteins IV." Journal of Chromatography A 1139, no. 1 (2007): 84–94. http://dx.doi.org/10.1016/j.chroma.2006.11.003.

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37

Haidacher, D., A. Vailaya, and C. Horvath. "Temperature effects in hydrophobic interaction chromatography." Proceedings of the National Academy of Sciences 93, no. 6 (1996): 2290–95. http://dx.doi.org/10.1073/pnas.93.6.2290.

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38

RACUSEN, DAVID. "PATATIN PURIFICATION BY HYDROPHOBIC INTERACTION CHROMATOGRAPHY." Journal of Food Biochemistry 13, no. 6 (1989): 453–56. http://dx.doi.org/10.1111/j.1745-4514.1989.tb00412.x.

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39

Schmidtchen, Artur, and Lars-Åke Fransson. "Hydrophobic interaction chromatography of fibroblast proteoglycans." Biomedical Chromatography 7, no. 1 (1993): 48–55. http://dx.doi.org/10.1002/bmc.1130070113.

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40

Roettger, Belinda F., Julia A. Myers, Michael R. Ladisch, and Fred E. Regnier. "Adsorption Phenomena in Hydrophobic Interaction Chromatography." Biotechnology Progress 5, no. 3 (1989): 79–88. http://dx.doi.org/10.1002/btpr.5420050304.

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41

Sudhakaran, Vayalombron K., and Jaiprakash G. Shewale. "Hydrophobic interaction chromatography of penicillin amidase." Biotechnology Letters 9, no. 8 (1987): 539–42. http://dx.doi.org/10.1007/bf01026657.

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42

Narhi, Linda Owers, Yoshiko Kita, and Tsutomu Arakawa. "Hydrophobic interaction chromatography in alkaline pH." Analytical Biochemistry 182, no. 2 (1989): 266–70. http://dx.doi.org/10.1016/0003-2697(89)90592-7.

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43

Cui, Xin, Jing Liu, Lei Xie, Jun Huang, and Hongbo Zeng. "Interfacial ion specificity modulates hydrophobic interaction." Journal of Colloid and Interface Science 578 (October 2020): 135–45. http://dx.doi.org/10.1016/j.jcis.2020.05.091.

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44

Müller, Egbert, Judith Vajda, Djuro Josic, Tim Schröder, Romain Dabre, and Tim Frey. "Mixed electrolytes in hydrophobic interaction chromatography†." Journal of Separation Science 36, no. 8 (2013): 1327–34. http://dx.doi.org/10.1002/jssc.201200704.

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45

Liu, Jinyuan, Mengdi Wang, Fan Feng, Annie Tang, Qiqin Le, and Bo Zhu. "Hydrophobic and Hydrophilic Solid-Fluid Interaction." ACM Transactions on Graphics 41, no. 6 (2022): 1–15. http://dx.doi.org/10.1145/3550454.3555478.

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We propose a novel solid-fluid coupling method to capture the subtle hydrophobic and hydrophilic interactions between liquid, solid, and air at their multi-phase junctions. The key component of our approach is a Lagrangian model that tackles the coupling, evolution, and equilibrium of dynamic contact lines evolving on the interface between surface-tension fluid and deformable objects. This contact-line model captures an ensemble of small-scale geometric and physical processes, including dynamic waterfront tracking, local momentum transfer and force balance, and interfacial tension calculation. On top of this contact-line model, we further developed a mesh-based level set method to evolve the three-phase T-junction on a deformable solid surface. Our dynamic contact-line model, in conjunction with its monolithic coupling system, unifies the simulation of various hydrophobic and hydrophilic solid-fluid-interaction phenomena and enables a broad range of challenging small-scale elastocapillary phenomena that were previously difficult or impractical to solve, such as the elastocapillary origami and self-assembly, dynamic contact angles of drops, capillary adhesion, as well as wetting and splashing on vibrating surfaces.
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46

Hassan, Ahmad, and Saad Rabbani. "Hydrophobic interaction chromatography and modeling of protein adsorption on hydrophobic gel." Asian Journal of Pharmaceutical Research 10, no. 4 (2020): 247–52. http://dx.doi.org/10.5958/2231-5691.2020.00043.x.

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47

Jafar, Husam Ali. "Hydrophobic Interaction Chromatography and Modeling of Protein Adsorption on Hydrophobic Gel." Brilliant Engineering 2, no. 1 (2020): 1–5. http://dx.doi.org/10.36937/ben.2021.001.001.

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In this work the thermodynamic model of Chen and Sun which describes the adsorption of protein on a hydrophobic gel in hydrophobic interaction chromatography process is modified by substitution activity instead of protein and salt concentration in liquid phase. The model is based on two-state equilibrium of protein in solution and adsorbed phase. Also, the effect of salt concentration and type of hydrophobic gel on the amount of protein adsorption is investigated. Finally, the accuracy of model is evaluated by measuring average absolute deviation (AAD) for adsorption isotherm in different salt concentration. The results show that the modified model had high accuracy for prediction the adsorption isotherm in different type of adsorbed and salt concentration.
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48

AKAHANE, Kenji, Yasuo NAGANO, and Hideaki UMEYAMA. "Hydrophobic effect on the protein-ligand interaction; Hydrophobic field-effect index and hydrophobic correlation index." CHEMICAL & PHARMACEUTICAL BULLETIN 37, no. 1 (1989): 86–92. http://dx.doi.org/10.1248/cpb.37.86.

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49

Dzisoo, Anthony Mackitz, Juanjuan Kang, Pengcheng Yao, Benjamin Klugah-Brown, Birga Anteneh Mengesha, and Jian Huang. "SSH: A Tool for Predicting Hydrophobic Interaction of Monoclonal Antibodies Using Sequences." BioMed Research International 2020 (June 2, 2020): 1–6. http://dx.doi.org/10.1155/2020/3508107.

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Therapeutic antibodies are one of the most important parts of the pharmaceutical industry. They are widely used in treating various diseases such as autoimmune diseases, cancer, inflammation, and infectious diseases. Their development process however is often brought to a standstill or takes a longer time and is then more expensive due to their hydrophobicity problems. Hydrophobic interactions can cause problems on half-life, drug administration, and immunogenicity at all stages of antibody drug development. Some of the most widely accepted and used technologies for determining the hydrophobic interactions of antibodies include standup monolayer adsorption chromatography (SMAC), salt-gradient affinity-capture self-interaction nanoparticle spectroscopy (SGAC-SINS), and hydrophobic interaction chromatography (HIC). However, to measure SMAC, SGAC-SINS, and HIC for hundreds of antibody drug candidates is time-consuming and costly. To save time and money, a predictor called SSH is developed. Based on the antibody’s sequence only, it can predict the hydrophobic interactions of monoclonal antibodies (mAbs). Using the leave-one-out crossvalidation, SSH achieved 91.226% accuracy, 96.396% sensitivity or recall, 84.196% specificity, 87.754% precision, 0.828 Mathew correlation coefficient (MCC), 0.919 f-score, and 0.961 area under the receiver operating characteristic (ROC) curve (AUC).
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50

Arakawa, Tsutomu, Masao Tokunaga, Takuya Maruyama, and Kentaro Shiraki. "Two Elution Mechanisms of MEP Chromatography." Current Protein & Peptide Science 20, no. 1 (2018): 28–33. http://dx.doi.org/10.2174/1389203718666171117105132.

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MEP (mercapto-ethyl-pyridine) HyperCel is one of the hydrophobic charge induction chromatography (HCIC) resins. Under normal operation, proteins are bound to the MEP resin at neutral pH, at which MEP is not charged, mostly via hydrophobic interaction. MEP has a pyridine group, whose pK is 4.8, and hence is positively charged at acidic pH range. Based on the binding mechanism (i.e., hydrophobic interaction) and the induced positive charge at acidic pH, there may be two ways to elute the bound proteins. One way is to bring the pH down to protonate both MEP resin and the bound protein, leading to charge repulsion and thereby elution. Another way is to use hydrophobic interaction modifiers, which are often used in hydrophobic interaction chromatography, to reduce hydrophobic interaction. Here, we summarize such two possible elution approaches.
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