ACS Publications. Most Trusted. Most Cited. Most Read

OR SEARCH CITATIONS

My Activity
Publications
CONTENT TYPES

Figure 1Loading Img
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Phys. Chem. B 2007, 111, 9, 2347-2356
RETURN TO ISSUEPREVArticleNEXT

Directed Assembly of Binary Monolayers with a High Protein Affinity:  Infrared Reflection Absorption Spectroscopy (IRRAS) and Surface Plasmon Resonance (SPR)

View Author Information
Key Laboratory of Mesoscopic Chemistry (Ministry of Education), State Key Laboratory of Coordination Chemistry, and School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210093, People's Republic of China
Cite this: J. Phys. Chem. B 2007, 111, 9, 2347–2356
Publication Date (Web):February 8, 2007
https://doi.org/10.1021/jp0653196
Copyright © 2007 American Chemical Society
Request reuse permissions

    Article Views

    458

    Altmetric

    -

    Citations

    34
    LEARN ABOUT THESE METRICS
    Other access options
    Get e-Alerts
    SUBJECTS:

    Abstract

    Infrared reflection absorption spectroscopy (IRRAS) and surface plasmon resonance (SPR) techniques have been employed to investigate human serum albumin (HSA) binding to binary monolayers of zwitterionic dipalmitoylphosphatidylcholine (DPPC) and cationic dioctadecyldimethylammonium bromide (DOMA). At the air−water interface, the favorable electrostatic interaction between DPPC and DOMA leads to a dense chain packing. The tilt angle of the hydrocarbon chains decreases with increasing mole fraction of DOMA (XDOMA) in the monolayers at the surface pressure 30 mN/m:  DPPC (∼30°), XDOMA = 0.1 (∼15°), and XDOMA = 0.3 (∼0°). Negligible protein binding to the DPPC monolayer is observed in contrast to a significant binding to the binary monolayers. After HSA binding, the hydrocarbon chains at XDOMA = 0.1 undergo an increase in tilt angle from 15° to 25∼30°, and the chains at XDOMA = 0.3 remain almost unchanged. The two components in the monolayers deliver through lateral reorganization, induced by the protein in the subphase, to form multiple interaction sites favorable for protein binding. The surfaces with a high protein affinity are created through the directed assembly of binary monolayers for use in biosensing.

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    *

     Corresponding author. E-mail:  [email protected]. Fax:  86-25-83317761.

    Cited By

    This article is cited by 34 publications.

    1. Mohd. Akram, Sana Anwar, Imtiyaz Ahmad Bhat, and Kabir-ud-Din . Multifaceted Analysis of the Noncovalent Interactions of Myoglobin with Finely Tuned Gemini Surfactants: A Comparative Study. Industrial & Engineering Chemistry Research 2017, 56 (46) , 13663-13676. https://doi.org/10.1021/acs.iecr.7b01583
    2. Xianfeng Zhang, Xuezhong Du, Xuan Huang, and Zhongpeng Lv . Creating Protein-Imprinted Self-Assembled Monolayers with Multiple Binding Sites and Biocompatible Imprinted Cavities. Journal of the American Chemical Society 2013, 135 (25) , 9248-9251. https://doi.org/10.1021/ja402423r
    3. Ignacio F. Gallardo and Lauren J. Webb. Tethering Hydrophobic Peptides to Functionalized Self-Assembled Monolayers on Gold through Two Chemical Linkers Using the Huisgen Cycloaddition. Langmuir 2010, 26 (24) , 18959-18966. https://doi.org/10.1021/la1036585
    4. Katarzyna Czapla, Beata Korchowiec and Ewa Rogalska . Differentiating Oxicam Nonsteroidal Anti-Inflammatory Drugs in Phosphoglyceride Monolayers. Langmuir 2010, 26 (5) , 3485-3492. https://doi.org/10.1021/la903052t
    5. Haifu Zheng and Xuezhong Du. Protein-Directed Spatial Rearrangement of Glycolipids at the Air−Water Interface for Bivalent Protein Binding: In Situ Infrared Reflection Absorption Spectroscopy. The Journal of Physical Chemistry B 2010, 114 (1) , 577-584. https://doi.org/10.1021/jp908559n
    6. Yung-Chung Chen, Tzong-Yuan Juang, Tzong-Ming Wu, Shenghong A. Dai, Wen-Jang Kuo, Ying-Ling Liu, Franklin M. C. Chen and Ru-Jong Jeng . Orderly Arranged NLO Materials Based on Chromophore-Containing Dendrons on Exfoliated Layered Templates. ACS Applied Materials & Interfaces 2009, 1 (10) , 2371-2381. https://doi.org/10.1021/am900499s
    7. Haifu Zheng and Xuezhong Du. Enhanced Binding and Biosensing of Carbohydrate-Functionalized Monolayers to Target Proteins by Surface Molecular Imprinting. The Journal of Physical Chemistry B 2009, 113 (32) , 11330-11337. https://doi.org/10.1021/jp9060279
    8. Carlos E. Román-Velázquez, Cecilia Noguez and Jin Z. Zhang. Theoretical Study of Surface Plasmon Resonances in Hollow Gold−Silver Double-Shell Nanostructures. The Journal of Physical Chemistry A 2009, 113 (16) , 4068-4074. https://doi.org/10.1021/jp810422r
    9. Katarzyna Wiȩcław, Beata Korchowiec, Yohann Corvis, Jacek Korchowiec, Hassan Guermouche and Ewa Rogalska. Meloxicam and Meloxicam-β-Cyclodextrin Complex in Model Membranes: Effects on the Properties and Enzymatic Lipolysis of Phospholipid Monolayers in Relation to Anti-inflammatory Activity. Langmuir 2009, 25 (3) , 1417-1426. https://doi.org/10.1021/la8033897
    10. Marie-Hélène Ropers, Annette Meister, Alfred Blume and Marie-Christine Ralet . Pectin−Lipid Assembly at the Air–Water Interface: Effect of the Pectin Charge Distribution. Biomacromolecules 2008, 9 (4) , 1306-1312. https://doi.org/10.1021/bm7013685
    11. Huijin Liu,, Xuezhong Du, and, Yan Li. Novel Metal Coordinations in the Monolayers of an Amino-Acid-Derived Schiff Base at the Air−Water Interface and Langmuir−Blodgett Films. The Journal of Physical Chemistry C 2007, 111 (45) , 17025-17031. https://doi.org/10.1021/jp074341b
    12. Huijin Liu,, Wangen Miao, and, Xuezhong Du. Determination of Chain Orientation in the Monolayers of Amino-Acid-Derived Schiff Base at the Air−Water Interface Using in Situ Infrared Reflection Absorption Spectroscopy. Langmuir 2007, 23 (22) , 11034-11041. https://doi.org/10.1021/la702017p
    13. Xuezhong Du,, Yuchun Wang,, Yuanhua Ding, and, Rong Guo. Protein-Directed Assembly of Binary Monolayers at the Interface and Surface Patterns of Protein on the Monolayers. Langmuir 2007, 23 (15) , 8142-8149. https://doi.org/10.1021/la700955f
    14. Sana Anwar, Mohammad Osama, Hira Lal, Kabir-ud-Din, Mohd. Akram. Gemini versus single-chain cationic surfactant-assisted unfolding of myoglobin and their ousting by β-cyclodextrin. Journal of Molecular Liquids 2023, 384 , 122227. https://doi.org/10.1016/j.molliq.2023.122227
    15. Cecilio Carrera, Manuel Felix, María Luisa López‐Castejón, Víctor Manuel Pizones. Understanding Interfacial Rheology in Food Emulsions. 2023, 57-72. https://doi.org/10.1002/9781119860594.ch4
    16. Cecilio Carrera Sánchez, Juan M. Rodríguez Patino. Contribution of the engineering of tailored interfaces to the formulation of novel food colloids. Food Hydrocolloids 2021, 119 , 106838. https://doi.org/10.1016/j.foodhyd.2021.106838
    17. Ankit D. Kanthe, Charles Maldarelli, Raymond Tu. Interfacial Behaviors of Proteins. 2021, 51-114. https://doi.org/10.1007/978-3-030-57177-1_3
    18. Shumin Cheng, Siyang Li, Narcisse T. Tsona, Christian George, Lin Du. Alterations in the surface properties of sea spray aerosols introduced by the presence of sterols. Science of The Total Environment 2019, 671 , 1161-1169. https://doi.org/10.1016/j.scitotenv.2019.03.433
    19. G. Vignesh, K. Sugumar, S. Arunachalam, S. Vignesh, R. Arthur James, R. Arun, K. Premkumar. Studies on the synthesis, characterization, human serum albumin binding and biological activity of single chain surfactant–cobalt(III) complexes. Luminescence 2016, 31 (2) , 523-532. https://doi.org/10.1002/bio.2991
    20. G. Vignesh, K. Sugumar, S. Arunachalam, S. Vignesh, R. Arthur James. A comparative study on the binding of single and double chain surfactant–cobalt(III) complexes with bovine serum albumin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2013, 113 , 415-422. https://doi.org/10.1016/j.saa.2013.04.123
    21. Haifu Zheng, Xuezhong Du. Reduced steric hindrance and optimized spatial arrangement of carbohydrate ligands in imprinted monolayers for enhanced protein binding. Biochimica et Biophysica Acta (BBA) - Biomembranes 2013, 1828 (2) , 792-800. https://doi.org/10.1016/j.bbamem.2012.11.006
    22. Yan Liu, Liu Yang, Rong Guo. Interaction between β-casein micelles and imidazolium-based ionic liquid surfactant. Soft Matter 2013, 9 (13) , 3671. https://doi.org/10.1039/c2sm27134f
    23. Li Yang, Zihua Zhu, Xiao-Ying Yu, Suntharampillai Thevuthasan, James P. Cowin. Performance of a microfluidic device for in situ ToF-SIMS analysis of selected organic molecules at aqueous surfaces. Analytical Methods 2013, 5 (10) , 2515. https://doi.org/10.1039/c3ay26513g
    24. Haifu Zheng, Xuezhong Du. Multivalent protein binding in carbohydrate-functionalized monolayers through protein-directed rearrangement and reorientation of glycolipids at the air–water interface. Biochimica et Biophysica Acta (BBA) - Biomembranes 2011, 1808 (9) , 2128-2135. https://doi.org/10.1016/j.bbamem.2011.04.019
    25. Yan Liu, Yang Liu, Rong Guo. Insights into cyclodextrin-modulated interactions between protein and surfactant at specific and nonspecific binding stages. Journal of Colloid and Interface Science 2010, 351 (1) , 180-189. https://doi.org/10.1016/j.jcis.2010.07.032
    26. Julia Maldonado-Valderrama, Juan M. Rodríguez Patino. Interfacial rheology of protein–surfactant mixtures. Current Opinion in Colloid & Interface Science 2010, 15 (4) , 271-282. https://doi.org/10.1016/j.cocis.2009.12.004
    27. Huamin Liang, Heini Miranto, Niko Granqvist, Janusz W. Sadowski, Tapani Viitala, Bochu Wang, Marjo Yliperttula. Surface plasmon resonance instrument as a refractometer for liquids and ultrathin films. Sensors and Actuators B: Chemical 2010, 149 (1) , 212-220. https://doi.org/10.1016/j.snb.2010.05.048
    28. Jin Zhang. Spectroscopic Methods. 2010, 6-1-6-36. https://doi.org/10.1201/9781420093551-c6
    29. Andreas Erbe, Andreas Kerth, Margitta Dathe, Alfred Blume. Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers. ChemBioChem 2009, 10 (18) , 2884-2892. https://doi.org/10.1002/cbic.200900444
    30. Julien Gravier, Beata Korchowiec, Raphaël Schneider, Ewa Rogalska. Interaction of amphiphilic chlorin-based photosensitizers with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monolayers. Chemistry and Physics of Lipids 2009, 158 (2) , 102-109. https://doi.org/10.1016/j.chemphyslip.2009.01.004
    31. Jin Z. Zhang, Cecilia Noguez. Plasmonic Optical Properties and Applications of Metal Nanostructures. Plasmonics 2008, 3 (4) , 127-150. https://doi.org/10.1007/s11468-008-9066-y
    32. Rebecca L. Rich, David G. Myszka. Survey of the year 2007 commercial optical biosensor literature. Journal of Molecular Recognition 2008, 21 (6) , 355-400. https://doi.org/10.1002/jmr.928
    33. Juan M. Rodríguez Patino, Cecilio Carrera Sánchez, Ma. Rosario Rodríguez Niño. Implications of interfacial characteristics of food foaming agents in foam formulations. Advances in Colloid and Interface Science 2008, 140 (2) , 95-113. https://doi.org/10.1016/j.cis.2007.12.007
    34. Juan M. Rodríguez Patino, Ma. Rosario Rodríguez Niño, Cecilio Carrera Sánchez. Physico-chemical properties of surfactant and protein films. Current Opinion in Colloid & Interface Science 2007, 12 (4-5) , 187-195. https://doi.org/10.1016/j.cocis.2007.06.003
    Download PDF

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect