1932

Abstract

Proteins at surfaces and interfaces play important roles in the function and performance of materials in applications ranging from diagnostic assays to biomedical devices. To improve the performance of these materials, detailed molecular structure (conformation and orientation) along with the identity and concentrations of the surface-bound proteins on those materials must be determined. This article describes radiolabeling, surface plasmon resonance, quartz crystal microbalance with dissipation, X-ray photoelectron spectroscopy, secondary ion mass spectrometry, sum frequency generation spectroscopy, and computational techniques along with the information each technique provides for characterizing protein films. A multitechnique approach using both experimental and computation methods is required for these investigations. Although it is now possible to gain much insight into the structure of surface-bound proteins, it is still not possible to obtain the same level of structural detail about proteins on surfaces as can be obtained about proteins in crystals and solutions, especially for large, complex proteins. However, recent results have shown it is possible to obtain detailed structural information (e.g., backbone and side chain orientation) about small peptides (5–20 amino sequences) on surfaces. Current studies are extending these investigations to small proteins such as protein G B1 (∼6 kDa). Approaches for furthering the capabilities for characterizing the molecular structure of surface-bound proteins are proposed.

Loading

Article metrics loading...

/content/journals/10.1146/annurev-anchem-091520-010206
2021-07-27
2024-05-02
Loading full text...

Full text loading...

/deliver/fulltext/anchem/14/1/annurev-anchem-091520-010206.html?itemId=/content/journals/10.1146/annurev-anchem-091520-010206&mimeType=html&fmt=ahah

Literature Cited

  1. 1. 
    Castner DG 2017. Biomedical surface analysis: evolution and future directions. Biointerphases 12:02C301
    [Google Scholar]
  2. 2. 
    Castner DG, Ratner BD 2002. Biomedical surface science: foundations to frontiers. Surface Sci 500:28–60
    [Google Scholar]
  3. 3. 
    Nudelman F, Sommerdijk NAJM 2012. Biomineralization as an inspiration for materials chemistry. Angew. Chem. Int. Ed. 51:6582–96
    [Google Scholar]
  4. 4. 
    Palmer LC, Newcomb CJ, Kaltz SR, Spoerke ED, Stupp SI 2008. Biomimetic systems for hydroxyapatite mineralization inspired by bone and enamel. Chem. Rev. 108:4754–83
    [Google Scholar]
  5. 5. 
    Weiner S, Addadi L 2011. Crystallization pathways in biomineralization. Annu. Rev. Mater. Res. 41:21–40
    [Google Scholar]
  6. 6. 
    Norde W, Horbett TA, Brash JL 2012. Proteins at interfaces III: introductory overview. Proteins at Interfaces III: State of the Art T Horbett, JL Brash, W Norde 1–34 Washington, DC: Am. Chem. Soc.
    [Google Scholar]
  7. 7. 
    Brash JL. 2000. Exploiting the current paradigm of blood–material interactions for the rational design of blood-compatible materials. J. Biomater. Sci. Polymer Ed. 11:1135–46
    [Google Scholar]
  8. 8. 
    Weidner T, Castner DG. 2013. SFG analysis of surface bound proteins: a route towards structure determination. Phys. Chem. Chem. Phys. 15:12516–24
    [Google Scholar]
  9. 9. 
    Michel R, Castner DG. 2006. Advances in time-of-flight secondary ion mass spectrometry analysis of protein films. Surface Interface Anal 38:1386–92
    [Google Scholar]
  10. 10. 
    Rupp B. 2009. Biomolecular Crystallography: Principles, Practice and Application to Structural Biology New York: Garland Sci.
  11. 11. 
    Cavanagh J, Fairbrother WJ, Palmer AG 3rd, Rance M, Skelton NJ. 2007. Protein NMR Spectroscopy: Principles and Practice Boston: Academic
  12. 12. 
    Hermanson GT. 2013. Bioconjugate Techniques Amsterdam: Elsevier
  13. 13. 
    Wagner MS, Castner DG. 2001. Characterization of adsorbed protein films by time-of-flight secondary ion mass spectrometry with principal component analysis. Langmuir 17:4649–60
    [Google Scholar]
  14. 14. 
    Wagner MS, Horbett TA, Castner DG. 2003. Characterizing multicomponent adsorbed protein films using electron spectroscopy for chemical analysis, time-of-flight secondary ion mass spectrometry, and radiolabeling: capabilities and limitations. Biomaterials 24:1897–908
    [Google Scholar]
  15. 15. 
    Baio JE, Graham DJ, Castner DG. 2020. Surface analysis tools for characterizing biological materials. Chem. Soc. Rev. 49:3278–96
    [Google Scholar]
  16. 16. 
    Horbett TA. 1981. Adsorption of proteins from plasma to a series of hydrophilic-hydrophobic co-polymers. II. Compositional analysis with the prelabeled protein technique. J. Biomed. Mater. Res. 15:673–95
    [Google Scholar]
  17. 17. 
    Horbett TA. 1986. Techniques for protein adsorption studies. Techniques of Biocompatibility Testing DF Williams 183–214 Boca Raton, FL: CRC Press
    [Google Scholar]
  18. 18. 
    Wijaya E, Lenaerts C, Maricot S, Hastanin J, Habraken S et al. 2011. Surface plasmon resonance-based biosensors: from the development of different SPR structures to novel surface functionalization strategies. Curr. Opin. Solid State Mater. Sci. 15:208–24
    [Google Scholar]
  19. 19. 
    Campbell CT, Kim G. 2007. SPR microscopy and its applications to high-throughput analyses of biomolecular binding events and their kinetics. Biomaterials 28:2380–92
    [Google Scholar]
  20. 20. 
    Rodahl M, Höök F, Krozer A, Brzezinski P, Kasemo B. 1995. Quartz-crystal microbalance setup for frequency and q-factor measurements in gaseous and liquid environments. Rev. Sci. Instrum. 66:3924–30
    [Google Scholar]
  21. 21. 
    Homola J, Vaisocherova H, Dostalek J, Piliarik M. 2005. Multi-analyte surface plasmon resonance biosensing. Methods 37:26–36
    [Google Scholar]
  22. 22. 
    Luan EX, Shoman H, Ratner DM, Cheung KC, Chrostowski L. 2018. Silicon photonic biosensors using label-free detection. Sensors 18:3519
    [Google Scholar]
  23. 23. 
    Anker JN, Hall WP, Lyandres O, Shah NC, Zhao J, Van Duyne RP. 2008. Biosensing with plasmonic nanosensors. Nat. Mater. 7:442–53
    [Google Scholar]
  24. 24. 
    Jung LS, Campbell CT, Chinowsky TM, Mar MN, Yee SS. 1998. Quantitative interpretation of the response of surface plasmon resonance sensors to adsorbed films. Langmuir 14:5636–48
    [Google Scholar]
  25. 25. 
    Jung LS, Nelson KE, Stayton PS, Campbell CT. 2000. Binding and dissociation kinetics of wild-type and mutant streptavidins on mixed biotin-containing alkylthiolate monolayers. Langmuir 16:9421–32
    [Google Scholar]
  26. 26. 
    Berquand A, Xia N, Castner DG, Clare BH, Abbott NL et al. 2005. Antigen binding forces of single antilysozyme Fv fragments explored by atomic force microscopy. Langmuir 21:5517–23
    [Google Scholar]
  27. 27. 
    Tamura GS, Hull JR, Oberg MD, Castner DG. 2006. High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity. Infect. Immunity 74:5739–46
    [Google Scholar]
  28. 28. 
    Sauerbrey G. 1959. Use of quartz vibration for weighing thin films on a microbalance. J. Phys. 155:206–12
    [Google Scholar]
  29. 29. 
    Höök F, Rodahl M, Brzezinski P, Kasemo B. 1998. Energy dissipation kinetics for protein and antibody-antigen adsorption under shear oscillation on a quartz crystal microbalance. Langmuir 14:729–34
    [Google Scholar]
  30. 30. 
    Ratner BD, Castner DG 2009. Electron spectroscopy for chemical analysis. Surface AnalysisThe Principal Techniques JC Vickerman, IS Gilmore 47–112 Chichester, UK: John Wiley & Sons. , 2nd ed..
    [Google Scholar]
  31. 31. 
    Easton CD, Kinnear C, McArthur SL, Gengenbach TR. 2020. Practical guides for X-ray photoelectron spectroscopy: analysis of polymers. J. Vac. Sci. Technol. A 38:023207
    [Google Scholar]
  32. 32. 
    Tidwell CD, Castner DG, Golledge SL, Ratner BD, Meyer K et al. 2001. Static time-of-flight secondary ion mass spectrometry and X-ray photoelectron spectroscopy characterization of adsorbed albumin and fibronectin films. Surface Interface Anal 31:724–33
    [Google Scholar]
  33. 33. 
    Michel R, Pasche S, Textor M, Castner DG. 2005. Influence of PEG architecture on protein adsorption and conformation. Langmuir 21:12327–32
    [Google Scholar]
  34. 34. 
    Ratner BD, Horbett TA, Shuttleworth D, Thomas HR. 1981. Analysis of the organization of protein films on solid-surfaces by ESCA. J. Colloid Interface Sci. 83:630–42
    [Google Scholar]
  35. 35. 
    Wagner MS, Horbett TA, Castner DG. 2003. Characterization of the structure of binary and ternary adsorbed protein films using electron spectroscopy for chemical analysis, time-of-flight secondary ion mass spectrometry, and radiolabeling. Langmuir 19:1708–15
    [Google Scholar]
  36. 36. 
    Tyler BJ, Castner DG, Ratner BD. 1989. Regularization—a stable and accurate method for generating depth profiles from angle-dependent XPS data. Surface Interface Anal 14:443–50
    [Google Scholar]
  37. 37. 
    Baugh L, Weidner T, Baio JE, Nguyen P-CT, Gamble LJ et al. 2010. Probing the orientation of surface-immobilized protein G B1 Using ToF-SIMS, sum frequency generation, and NEXAFS spectroscopy. Langmuir 26:16434–41
    [Google Scholar]
  38. 38. 
    Fletcher JS. 2015. Latest applications of 3D ToF-SIMS bio-imaging. Biointerphases 10:018902
    [Google Scholar]
  39. 39. 
    Vickerman JC 2009. Molecular surface mass spectrometry by SIMS. Surface Analysis—The Principal Techniques JC Vickerman, IS Gilmore 113–205 Chichester, UK: John Wiley & Sons. , 2nd ed..
    [Google Scholar]
  40. 40. 
    Winograd N. 2015. Imaging mass spectrometry on the nanoscale with cluster ion beams. Anal. Chem. 87:328–33
    [Google Scholar]
  41. 41. 
    Robinson MA, Graham DJ, Castner DG. 2012. ToF-SIMS depth profiling of cells: z-correction, 3D imaging, and sputter rate of individual NIH/3T3 fibroblasts. Anal. Chem. 84:4880–85
    [Google Scholar]
  42. 42. 
    Yamada I, Matsuo J, Toyoda N, Kirkpatrick A. 2001. Materials processing by gas cluster ion beams. Mater. Sci. Eng. R 34:231–95
    [Google Scholar]
  43. 43. 
    Delcorte A, Delmez V, Dupont-Gillain C, Lauzin C, Jefford H et al. 2020. Large cluster ions: soft local probes and tools for organic and bio surfaces. Phys. Chem. Chem. Phys. 22:17427–47
    [Google Scholar]
  44. 44. 
    Gilmore IS. 2013. SIMS of organics—advances in 2D and 3D imaging and future outlook. J. Vac. Sci. Technol. A 31:050819
    [Google Scholar]
  45. 45. 
    Mantus DS, Ratner BD, Carlson BA, Moulder JF. 1993. Static secondary-ion mass-spectrometry of adsorbed proteins. Anal. Chem. 65:1431–38
    [Google Scholar]
  46. 46. 
    Foster RN, Harrison ET, Castner DG. 2016. ToF-SIMS and XPS characterization of protein films adsorbed onto bare and sodium styrene sulfonate grafted gold substrates. Langmuir 32:3207–16
    [Google Scholar]
  47. 47. 
    Killian MS, Taylor AJ, Castner DG. 2018. Stabilization of dry protein coatings with compatible solutes. Biointerphases 13:06E401
    [Google Scholar]
  48. 48. 
    Xia N, Castner DG. 2003. Preserving the structure of adsorbed protein films for time-of-flight secondary ion mass spectrometry analysis. J. Biomed. Mater. Res. Part A 67A:179–90
    [Google Scholar]
  49. 49. 
    Graham DJ, Castner DG. 2012. Multivariate analysis of ToF-SIMS data from multicomponent systems: the why, when, and how. Biointerphases 7:49
    [Google Scholar]
  50. 50. 
    Graham DJ, Wagner MS, Castner DG. 2006. Information from complexity: challenges of TOF-SIMS data interpretation. Appl. Surface Sci. 252:6860–68
    [Google Scholar]
  51. 51. 
    Wagner MS, Tyler BJ, Castner DG. 2002. Interpretation of static time-of-flight secondary ion mass spectra of adsorbed protein films by multivariate pattern recognition. Anal. Chem. 74:1824–35
    [Google Scholar]
  52. 52. 
    Tyler BJ, Rayal G, Castner DG. 2007. Multivariate analysis strategies for processing ToF-SIMS images of biomaterials. Biomaterials 28:2412–23
    [Google Scholar]
  53. 53. 
    Sanni OD, Wagner MS, Briggs D, Castner DG, Vickerman JC. 2002. Classification of adsorbed protein static ToF-SIMS spectra by principal component analysis and neural networks. Surface Interface Anal 33:715–28
    [Google Scholar]
  54. 54. 
    Welch NG, Madiona RMT, Payten TB, Jones RT, Brack N et al. 2016. Surface adsorbed antibody characterization using ToF-SIMS with principal component analysis and artificial neural networks. Langmuir 32:8717–28
    [Google Scholar]
  55. 55. 
    Robinson MA, Castner DG. 2013. Characterization of sample preparation methods of NIH/3T3 fibro-blasts for ToF-SIMS analysis. Biointerphases 8:15
    [Google Scholar]
  56. 56. 
    Johansson PK, Schmuser L, Castner DG. 2018. Nonlinear optical methods for characterization of molecular structure and surface chemistry. Top. Catal. 61:1101–24
    [Google Scholar]
  57. 57. 
    Hosseinpour S, Roeters SJ, Bonn M, Peukert W, Woutersen S, Weidner T. 2020. Structure and dynamics of interfacial peptides and proteins from vibrational sum-frequency generation spectroscopy. Chem. Rev. 120:3420–65
    [Google Scholar]
  58. 58. 
    Ye S, Nguyen KT, Le Clair SV, Chen Z. 2009. In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy. J. Struct. Biol. 168:61–77
    [Google Scholar]
  59. 59. 
    Yan ECY, Wang Z, Fu L. 2015. Proteins at interfaces probed by chiral vibrational sum frequency generation spectroscopy. J. Phys. Chem. B 119:2769–85
    [Google Scholar]
  60. 60. 
    Wang J, Clarke ML, Chen X, Even MA, Johnson WC, Chen Z. 2005. Molecular studies on protein conformations at polymer/liquid interfaces using sum frequency generation vibrational spectroscopy. Surface Sci 587:1–11
    [Google Scholar]
  61. 61. 
    Weidner T, Apte JS, Gamble LJ, Castner DG. 2010. Probing the orientation and conformation of α-helix and β-strand model peptides on self-assembled monolayers using sum frequency generation and NEXAFS spectroscopy. Langmuir 26:3433–40
    [Google Scholar]
  62. 62. 
    Weidner T, Breen NF, Li K, Drobny GP, Castner DG. 2010. Sum frequency generation and solid-state NMR study of the structure, orientation, and dynamics of polystyrene-adsorbed peptides. PNAS 107:13288–93
    [Google Scholar]
  63. 63. 
    Weidner T, Breen NF, Drobny GP, Castner DG. 2009. Amide or amine: determining the origin of the 3300 cm−1 NH mode in protein SFG spectra using 15N isotope labels. J. Phys. Chem. B 113:15423–26
    [Google Scholar]
  64. 64. 
    Mermut O, Phillips DC, York RL, McCrea KR, Ward RS, Somorjai GA. 2006. In situ adsorption studies of a 14-amino acid leucine-lysine peptide onto hydrophobic polystyrene and hydrophilic silica surfaces using quartz crystal microbalance, atomic force microscopy, and sum frequency generation vibrational spectroscopy. J. Am. Chem. Soc. 128:3598–607
    [Google Scholar]
  65. 65. 
    Fu L, Ma G, Yan ECY 2010. In situ misfolding of human islet amyloid polypeptide at interfaces probed by vibrational sum frequency generation. J. Am. Chem. Soc. 132:5405–12
    [Google Scholar]
  66. 66. 
    Ho J-J, Ghosh A, Zhang TO, Zanni MT. 2018. Heterogeneous amyloid β-sheet polymorphs identified on hydrogen bond promoting surfaces using 2D SFG spectroscopy. J. Phys. Chem. A 122:1270–82
    [Google Scholar]
  67. 67. 
    Engel MFM, vandenAkker CC, Schleeger M, Velikov KP, Koenderink GH, Bonn M 2012. The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution. J. Am. Chem. Soc. 134:14781–88
    [Google Scholar]
  68. 68. 
    Chen X, Chen Z. 2006. SFG studies on interactions between antimicrobial peptides and supported lipid bilayers. Biochim. Biophys. Acta 1758:1257–73
    [Google Scholar]
  69. 69. 
    Chen X, Wang J, Sniadecki JJ, Even MA, Chen Z 2005. Probing α-helical and β-sheet structures of peptides at solid/liquid interfaces with SFG. Langmuir 21:2662–64
    [Google Scholar]
  70. 70. 
    Roeters SJ, van Dijk CN, Torres-Knoop A, Backus EHG, Campen RK et al. 2013. Determining in situ protein conformation and orientation from the amide-I sum-frequency generation spectrum: theory and experiment. J. Phys. Chem. A 117:6311–22
    [Google Scholar]
  71. 71. 
    Schach D, Globisch C, Roeters SJ, Woutersen S, Fuchs A et al. 2014. Sticky water surfaces: helix-coil transitions suppressed in a cell-penetrating peptide at the air-water interface. J. Chem. Phys. 141:22D517
    [Google Scholar]
  72. 72. 
    Breen NF, Weidner T, Li K, Castner DG, Drobny GP. 2009. A solid-state deuterium NMR and sum-frequency generation study of the side-chain dynamics of peptides adsorbed onto surfaces. J. Am. Chem. Soc. 131:14148–49
    [Google Scholar]
  73. 73. 
    Lutz H, Jaeger V, Schmüser L, Bonn M, Pfaendtner J, Weidner T. 2017. The structure of the diatom silaffin peptide R5 within freestanding two-dimensional biosilica sheets. Angew. Chem. Int. Ed. 56:8277–80
    [Google Scholar]
  74. 74. 
    Lu H, Lutz H, Roeters SJ, Hood MA, Schäfer A et al. 2018. Calcium-induced molecular rearrangement of peptide folds enables biomineralization of vaterite calcium carbonate. J. Am. Chem. Soc. 140:2793–96
    [Google Scholar]
  75. 75. 
    Lu H, Schäfer A, Lutz H, Roeters SJ, Lieberwirth I et al. 2019. Peptide-controlled assembly of macroscopic calcium oxalate nanosheets. J. Phys. Chem. Lett. 10:2170–74
    [Google Scholar]
  76. 76. 
    Harrison ET, Weidner T, Castner DG, Interlandi G. 2017. Predicting the orientation of protein G B1 on hydrophobic surfaces using Monte Carlo simulations. Biointerphases 12:02D401
    [Google Scholar]
  77. 77. 
    Roeters SJ, Tronic EH, Baio JE, Castner DG, Weidner T. 2018. Structure of von Willebrand factor A1 on polystyrene determined from experimental and calculated sum frequency generation spectra. Biointerphases 13:06E411
    [Google Scholar]
  78. 78. 
    Xiong W, Laaser JE, Mehlenbacher RD, Zanni MT. 2011. Adding a dimension to the infrared spectra of interfaces using heterodyne detected 2D sum-frequency generation (HD 2D SFG) spectroscopy. PNAS 108:20902–7
    [Google Scholar]
  79. 79. 
    Laaser JE, Zanni MT. 2013. Extracting structural information from the polarization dependence of one- and two-dimensional sum frequency generation spectra. J. Phys. Chem. A 117:5875–90
    [Google Scholar]
  80. 80. 
    Laaser JE, Skoff DR, Ho J-J, Joo Y, Serrano AL et al. 2014. Two-dimensional sum-frequency generation reveals structure and dynamics of a surface-bound peptide. J. Am. Chem. Soc. 136:956–62
    [Google Scholar]
  81. 81. 
    Tan J, Zhang J, Li C, Luo Y, Ye S. 2019. Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules. Nat. Commun. 10:1010
    [Google Scholar]
  82. 82. 
    Pandey R, Usui K, Livingstone RA, Fischer SA, Pfaendtner J et al. 2016. Ice-nucleating bacteria control the order and dynamics of interfacial water. Sci. Adv. 2:e1501630
    [Google Scholar]
  83. 83. 
    Donovan MA, Lutz H, Yimer YY, Pfaendtner J, Bonn M, Weidner T. 2017. LK peptide side chain dynamics at interfaces are independent of secondary structure. Phys. Chem. Chem. Phys. 19:28507–11
    [Google Scholar]
  84. 84. 
    Latour RA. 2008. Molecular simulation of protein-surface interactions: benefits, problems, solutions, and future directions. Biointerphases 3:FC2–12
    [Google Scholar]
  85. 85. 
    Hildebrand N, Wei G, Köppen S, Colombi Ciacchi L 2018. Simulated and experimental force spectroscopy of lysozyme on silica. Phys. Chem. Chem. Phys. 20:19595–605
    [Google Scholar]
  86. 86. 
    Lutz H, Jaeger V, Berger R, Bonn M, Pfaendtner J, Weidner T. 2015. Biomimetic growth of ultrathin silica sheets using artificial amphiphilic peptides. Adv. Mater. Interfaces 2:1500282
    [Google Scholar]
  87. 87. 
    Lutz H, Jaeger V, Bonn M, Pfaendtner J, Weidner T. 2017. Acetylation dictates the morphology of nanophase biosilica precipitated by a 14-amino acid leucine–lysine peptide. J. Peptide Sci. 23:141–47
    [Google Scholar]
  88. 88. 
    Makrodimitris K, Masica DL, Kim ET, Gray JJ. 2007. Structure prediction of protein−solid surface interactions reveals a molecular recognition motif of statherin for hydroxyapatite. J. Am. Chem. Soc. 129:13713–22
    [Google Scholar]
  89. 89. 
    Qiu Y, Hudait A, Molinero V. 2019. How size and aggregation of ice-binding proteins control their ice nucleation efficiency. J. Am. Chem. Soc. 141:7439–52
    [Google Scholar]
  90. 90. 
    Chien YC, Masica DL, Gray JJ, Nguyen S, Vali H, McKee MD. 2009. Modulation of calcium oxalate dihydrate growth by selective crystal-face binding of phosphorylated osteopontin and polyaspartate peptide showing occlusion by sectoral (compositional) zoning. J. Biol. Chem. 284:23491–501
    [Google Scholar]
  91. 91. 
    Buckle EL, Prakash A, Bonomi M, Sampath J, Pfaendtner J, Drobny GP. 2019. Solid-state NMR and MD study of the structure of the statherin mutant SNa15 on mineral surfaces. J. Am. Chem. Soc. 141:1998–2011
    [Google Scholar]
  92. 92. 
    Alamdari S, Pfaendtner J. 2020. Impact of glutamate carboxylation in the adsorption of the α-1 domain of osteocalcin to hydroxyapatite and titania. Mol. Syst. Des. Eng. 5:620–31
    [Google Scholar]
  93. 93. 
    Pacella MS, Koo DCE, Thottungal RA, Gray JJ. 2013. Using the RosettaSurface algorithm to predict protein structure at mineral surfaces. Methods Enzymol. 532:343–66
    [Google Scholar]
  94. 94. 
    Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ. 2010. Toward a structure determination method for biomineral-associated protein using combined solid-state NMR and computational structure prediction. Structure 18:1678–87
    [Google Scholar]
  95. 95. 
    Collier G, Vellore NA, Yancey JA, Stuart SJ, Latour RA. 2012. Comparison between empirical protein force fields for the simulation of the adsorption behavior of structured LK peptides on functionalized surfaces. Biointerphases 7:24
    [Google Scholar]
  96. 96. 
    Deighan M, Pfaendtner J. 2013. Exhaustively sampling peptide adsorption with metadynamics. Langmuir 29:7999–8009
    [Google Scholar]
  97. 97. 
    Ma X, Zhang S, Jiao F, Newcomb CJ, Zhang Y et al. 2017. Tuning crystallization pathways through sequence engineering of biomimetic polymers. Nat. Mater. 16:767–74
    [Google Scholar]
  98. 98. 
    Beckner W, He Y, Pfaendtner J. 2016. Chain flexibility in self-assembled monolayers affects protein adsorption and surface hydration: a molecular dynamics study. J. Phys. Chem. B 120:10423–32
    [Google Scholar]
  99. 99. 
    Palunas K, Sprenger KG, Weidner T, Pfaendtner J. 2017. Effect of an ionic liquid/air interface on the structure and dynamics of amphiphilic peptides. J. Mol. Liquids 236:404–13
    [Google Scholar]
  100. 100. 
    Sprenger KG, Prakash A, Drobny G, Pfaendtner J. 2018. Investigating the role of phosphorylation in the binding of silaffin peptide R5 to silica with molecular dynamics simulations. Langmuir 34:1199–207
    [Google Scholar]
  101. 101. 
    Apte JS, Collier G, Latour RA, Gamble LJ, Castner DG. 2010. XPS and ToF-SIMS investigation of α-helical and β-strand peptide adsorption onto SAMs. Langmuir 26:3423–32
    [Google Scholar]
  102. 102. 
    Gibson CM, Diaz L, Kandarpa K, Sacks FM, Pasternak RC et al. 1993. Relation of vessel wall shear stress to atherosclerosis progression in human coronary arteries. Arterioscler. Thromb. 13:310–15
    [Google Scholar]
  103. 103. 
    Variola F. 2015. Atomic force microscopy in biomaterials surface science. Phys. Chem. Chem. Phys. 17:2950–59
    [Google Scholar]
  104. 104. 
    Leung C, Maradan D, Kramer A, Howorka S, Mesquida P, Hoogenboom BW. 2010. Improved Kelvin probe force microscopy for imaging individual DNA molecules on insulating surfaces. Appl. Phys. Lett. 97:203703
    [Google Scholar]
  105. 105. 
    Salerno M, Dante S 2018. Scanning Kelvin probe microscopy: challenges and perspectives towards increased application on biomaterials and biological samples. Materials 11:951
    [Google Scholar]
  106. 106. 
    Pilling M, Gardner P. 2016. Fundamental developments in infrared spectroscopic imaging for biomedical applications. Chem. Soc. Rev. 45:1935–57
    [Google Scholar]
  107. 107. 
    Ruggeri FS, Longo G, Faggiano S, Lipiec E, Pastore A, Dietler G. 2015. Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation. Nat. Commun. 6:7831
    [Google Scholar]
  108. 108. 
    Berweger S, Nguyen DM, Muller EA, Bechtel HA, Perkins TT, Raschke MB. 2013. Nano-chemical infrared imaging of membrane proteins in lipid bilayers. J. Am. Chem. Soc. 135:18292–95
    [Google Scholar]
  109. 109. 
    Marcott C, Lo M, Kjoller K, Fiat F, Baghdadli N et al. 2014. Localization of human hair structural lipids using nanoscale infrared spectroscopy and imaging. Appl. Spectrosc. 68:564–69
    [Google Scholar]
  110. 110. 
    Sereda G, VanLaecken A, Turner JA. 2019. Monitoring demineralization and remineralization of human dentin by characterization of its structure with resonance-enhanced AFM-IR chemical mapping, nanoindentation, and SEM. Dent. Mater. 35:617–26
    [Google Scholar]
  111. 111. 
    Paynter RW, Ratner BD, Horbett TA, Thomas HR. 1984. XPS studies on the organization of adsorbed protein films on fluoropolymers. J. Colloid Interface Sci. 101:233–45
    [Google Scholar]
  112. 112. 
    Ray S, Shard AG. 2011. Quantitative analysis of adsorbed proteins by X-ray photoelectron spectroscopy. Anal. Chem. 83:8659–66
    [Google Scholar]
  113. 113. 
    Belsey NA, Shard AG, Minelli C. 2015. Analysis of protein coatings on gold nanoparticles by XPS and liquid-based particle sizing techniques. Biointerphases 10:019012
    [Google Scholar]
  114. 114. 
    Muramoto S, Graham DJ, Wagner MS, Lee TG, Moon DW, Castner DG. 2011. ToF-SIMS analysis of adsorbed proteins: principal component analysis of the primary ion species effect on the protein fragmentation patterns. J. Phys. Chem. C 115:24247–55
    [Google Scholar]
  115. 115. 
    Kim YP, Hong MY, Kim J, Oh E, Shon HK et al. 2007. Quantitative analysis of surface-immobilized protein by TOF-SIMS: effects of protein orientation and trehalose additive. Anal. Chem. 79:1377–85
    [Google Scholar]
  116. 116. 
    Xia N, May CJ, McArthur SL, Castner DG. 2002. Time-of-flight secondary ion mass spectrometry analysis of conformational changes in adsorbed protein films. Langmuir 18:4090–97
    [Google Scholar]
  117. 117. 
    Wang H, Castner DG, Ratner BD, Jiang SY. 2004. Probing the orientation of surface-immobilized immunoglobulin G by time-of-flight secondary ion mass spectrometry. Langmuir 20:1877–87
    [Google Scholar]
  118. 118. 
    Lhoest JB, Detrait E, van den Bosch de Aguilar P, Bertrand P. 1998. Fibronectin adsorption, conformation, and orientation on polystyrene substrates studied by radiolabeling, XPS, and ToF SIMS. J. Biomed. Mater. Res. 41:95–103
    [Google Scholar]
  119. 119. 
    Henry M, Dupont-Gillain C, Bertrand P. 2003. Conformation change of albumin adsorbed on polycarbonate membranes as revealed by ToF-SIMS. Langmuir 19:6271–76
    [Google Scholar]
  120. 120. 
    Baio JE, Weidner T, Baugh L, Gamble LJ, Stayton PS, Castner DG. 2012. Probing the orientation of electrostatically immobilized protein G B1 by time-of-flight secondary ion spectrometry, sum frequency generation, and near-edge X-ray adsorption fine structure spectroscopy. Langmuir 28:2107–12
    [Google Scholar]
  121. 121. 
    Baio JE, Weidner T, Samuel NT, McCrea K, Baugh L et al. 2010. Multitechnique characterization of adsorbed peptide and protein orientation: LK310 and Protein G B1. J. Vac. Sci. Technol. B 28:C5D1–D8
    [Google Scholar]
  122. 122. 
    Dubey M, Emoto K, Takahashi H, Castner DG, Grainger DW. 2009. Affinity-based protein surface pattern formation by ligand self-selection from mixed protein solutions. Adv. Funct. Mater. 19:3046–55
    [Google Scholar]
  123. 123. 
    Liu F, Dubey M, Takahashi H, Castner DG, Grainger DW. 2010. Immobilized antibody orientation analysis using secondary ion mass spectrometry and fluorescence imaging of affinity-generated patterns. Anal. Chem. 82:2947–58
    [Google Scholar]
  124. 124. 
    Harrison ET, Wang Y-C, Carter L, Castner DG 2020. Characterizing protein G B1 orientation and its effect on IgG antibody binding using XPS, ToF-SIMS and QCM-D. Biointerphases 15:021002
    [Google Scholar]
  125. 125. 
    Nguyen KT, Le Clair SV, Ye S, Chen Z 2009. Orientation determination of protein helical secondary structures using linear and nonlinear vibrational spectroscopy. J. Phys. Chem. B 113:12169–80
    [Google Scholar]
  126. 126. 
    Hennig R, Heidrich J, Saur M, Schmüser L, Roeters SJ et al. 2015. IM30 triggers membrane fusion in cyanobacteria and chloroplasts. Nat. Commun. 6:7018
    [Google Scholar]
  127. 127. 
    Golbek TW, Padmanarayana M, Roeters SJ, Weidner T, Johnson CP, Baio JE. 2019. Otoferlin C2F domain-induced changes in membrane structure observed by sum frequency generation. Biophys. J. 117:1820–30
    [Google Scholar]
  128. 128. 
    Bellucci L, Ardèvol A, Parrinello M, Lutz H, Lu H et al. 2016. The interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptide. Nanoscale 8:8737–48
    [Google Scholar]
  129. 129. 
    Alamdari S, Roeters S, Golbek TW, Schmüser L, Weidner T, Pfaendtner J. 2020. Orientation and conformation of proteins at the air-water interface determined from integrative molecular dynamics simulations and sum frequency generation spectroscopy. Langmuir 36:11855–65
    [Google Scholar]
  130. 130. 
    Fu L, Wang Z, Psciuk BT, Xiao D, Batista VS, Yan ECY 2015. Characterization of parallel β-sheets at interfaces by chiral sum frequency generation spectroscopy. J. Phys. Chem. Lett. 6:1310–15
    [Google Scholar]
  131. 131. 
    Simpson GJ. 2004. Molecular origins of the remarkable chiral sensitivity of second-order nonlinear optics. Chem. Phys. Chem. 5:1301–10
    [Google Scholar]
  132. 132. 
    Ji N, Shen Y-R. 2006. A novel spectroscopic probe for molecular chirality. Chirality 18:146–58
    [Google Scholar]
  133. 133. 
    Wei F, Xu Y-Y, Guo Y, Liu S-L, Wang H-F. 2009. Quantitative surface chirality detection with sum frequency generation vibrational spectroscopy: twin polarization angle approach. Chin. J. Chem. Phys 22:592
    [Google Scholar]
  134. 134. 
    Perets EA, Yan ECY. 2019. Chiral water superstructures around antiparallel β-sheets observed by chiral vibrational sum frequency generation spectroscopy. J. Phys. Chem. Lett. 10:3395–401
    [Google Scholar]
  135. 135. 
    Tan J, Zhang J, Luo Y, Ye S. 2019. Misfolding of a human islet amyloid polypeptide at the lipid membrane populates through β-sheet conformers without involving α-helical intermediates. J. Am. Chem. Soc. 141:1941–48
    [Google Scholar]
  136. 136. 
    Meister K, Bäumer A, Szilvay GR, Paananen A, Bakker HJ. 2016. Self-assembly and conformational changes of hydrophobin classes at the air-water interface. J. Phys. Chem. Lett. 7:4067–71
    [Google Scholar]
  137. 137. 
    Schmüser L, Roeters S, Lutz H, Woutersen S, Bonn M, Weidner T. 2017. Determination of absolute orientation of protein α-helices at interfaces using phase-resolved sum frequency generation spectroscopy. J. Phys. Chem. Lett. 8:3101–5
    [Google Scholar]
  138. 138. 
    Okuno M, Ishibashi T-A. 2014. Chirality discriminated by heterodyne-detected vibrational sum frequency generation. J. Phys. Chem. Lett. 5:2874–78
    [Google Scholar]
  139. 139. 
    Okuno M, Ishibashi T-A. 2015. Heterodyne-detected achiral and chiral vibrational sum frequency generation of proteins at air/water interface. J. Phys. Chem. C 119:9947–54
    [Google Scholar]
  140. 140. 
    Kotowska AM, Trindade GF, Mendes PM, Williams PM, Aylott JW et al. 2020. Protein identification by 3D OrbiSIMS to facilitate in situ mapping and depth profiling. Nat. Commun. 11:5832
    [Google Scholar]
  141. 141. 
    de Beer AGF, Roke S 2007. Sum frequency generation scattering from the interface of an isotropic particle: geometrical and chiral effects. Phys. Rev. B 75:245438
    [Google Scholar]
  142. 142. 
    Roke S, Bonn M, Petukhov AV. 2004. Nonlinear optical scattering: the concept of effective susceptibility. Phys. Rev. B 70:115106
    [Google Scholar]
  143. 143. 
    Johansson PK, Castner DG. 2019. Vibrational sum-frequency scattering as a sensitive approach to detect structural changes in collagen fibers treated with surfactants. Langmuir 35:7848–57
    [Google Scholar]
  144. 144. 
    Shaw WJ, Long JR, Dindot JL, Campbell AA, Stayton PS, Drobny GP. 2000. Determination of statherin N-terminal peptide conformation on hydroxyapatite crystals. J. Am. Chem. Soc. 122:1709–16
    [Google Scholar]
  145. 145. 
    Weidner T, Dubey M, Breen NF, Ash J, Baio JE et al. 2012. Direct observation of phenylalanine orientations in statherin bound to hydroxyapatite surfaces. J. Am. Chem. Soc. 134:8750–53
    [Google Scholar]
  146. 146. 
    Roehrich A, Drobny G. 2013. Solid-state NMR studies of biomineralization peptides and proteins. Acc. Chem. Res. 46:2136–44
    [Google Scholar]
  147. 147. 
    Yeates TO, Agdanowski MP, Liu YX. 2020. Development of imaging scaffolds for cryo-electron microscopy. Curr. Opin. Struct. Biol. 60:142–49
    [Google Scholar]
/content/journals/10.1146/annurev-anchem-091520-010206
Loading
/content/journals/10.1146/annurev-anchem-091520-010206
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error