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Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces
Open accessAbstract
Atomic force microscopy (AFM) was used to directly measure the adhesion forces between three test proteins and low density polyethylene (LDPE) surfaces treated by glow discharge plasma to yield various levels of water wettability. The adhesion of proteins to the LDPE substrates showed a step dependence on the wettability of surfaces as measured by the water contact angle (theta). For LDPE surfaces with theta> approximately 60-65 degrees , stronger adhesion forces were observed for bovine serum albumin, fibrinogen and human FXII than for the surfaces with theta<60 degrees . Smaller adhesion forces were observed for FXII than for the other two proteins on all surfaces although trends were identical. Increasing the contact time from 0 to 50s for each protein-surface combination increased the adhesion force regardless of surface wettability. Time varying adhesion data was fit to an exponential model and free energies of protein unfolding were calculated. This data, viewed in light of previously published studies, suggests a 2-step model of protein denaturation, an early stage on the order of seconds to minutes where the outer surface of the protein interacts with the substrate and a second stage involving movement of hydrophobic amino acids from the protein core to the protein/surface interface. Impact statement: The work described in this manuscript shows a stark transition between protein adherent and protein non-adherent materials in the range of water contact angles 60-65 degrees , consistent with known changes in protein adsorption and activity. Time-dependent changes in adhesion force were used to calculate unfolding energies relating to protein-surface interactions. This analysis provides justification for a 2-step model of protein denaturation on surfaces.
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“Albeit it is most prominently active in the earlier stages where it affects platelet accumulation, coagulation, protein adsorption, and cell adhesion,[ 156 ]”
From Unraveling and Harnessing the Immune Response at the Cell–Biomaterial Interface for Tissue Engineering Purposes (2024) · cites this paper as [156]
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“This process—known as the Vroman effect—can vary in protein composition and time course for different implanted materials, leading to differences in FBR across different materials even at this early stage (Wilson et al., 2005; Xu and Siedlecki, 2007).”
From Foreign Body Reaction to Implanted Biomaterials and Its Impact in Nerve Neuroprosthetics (2021) · cites this paper as Xu and Siedlecki, 2007
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“As previously indicated, these adsorbed proteins may desorb rapidly, i.e. the Vroman Effect, and thus present time-dependent variations in the type and level of proteins cells encounter in the in vivo environment.[15]”
From Foreign body reaction to biomaterials (2008) · cites this paper as [15]
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Cites
A Survey of Structure−Property Relationships of Surfaces that Resist the Adsorption of Protein
Ostuni, E., Chapman, R. G., Holmlin, R. E., Takayama, S., & Whitesides, G. M. (2001) · Langmuir · doi:10.1021/la010384m · Cited by 1,799
Interpretation of Protein Adsorption: Surface-Induced Conformational Changes
Roach, P., Farrar, D. F., & Perry, C. C. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042898o · Cited by 1,487
Biological Responses to Materials
Anderson, J. M. (2001) · Annual Review of Materials Research · doi:10.1146/annurev.matsci.31.1.81 · Cited by 1,465
Role of hydration and water structure in biological and colloidal interactions
Israelachvili, J. N., & Wennerström, H. (1996) · Nature · doi:10.1038/379219a0 · Cited by 1,371
Biomedical surface science: Foundations to frontiers
Castner, D. G., & Ratner, B. D. (2002) · Surface Science · doi:10.1016/s0039-6028(01)01587-4 · Cited by 1,329
Zwitterionic SAMs that Resist Nonspecific Adsorption of Protein from Aqueous Buffer
Holmlin, R. E., Chen, X., Chapman, R., Takayama, S., & Whitesides, G. M. (2001) · Langmuir · doi:10.1021/la0015258 · Cited by 892
Globular proteins at solid/liquid interfaces
Haynes, C. A., & Norde, W. (1994) · Colloids and Surfaces B Biointerfaces · doi:10.1016/0927-7765(94)80066-9 · Cited by 849
Effect of Surface Wettability on the Adsorption of Proteins and Detergents
Sigal, G. B., Mrksich, M., & Whitesides, G. M. (1998) · Journal of the American Chemical Society · doi:10.1021/ja970819l · Cited by 817
Faucheux, N., Schweiss, R., Lützow, K., Werner, C., & Groth, T. (2003) · Biomaterials · doi:10.1016/j.biomaterials.2003.09.069 · Cited by 743
FTIR/ATR for protein adsorption to biomaterial surfaces
Chittur, K. K. (1998) · Biomaterials · doi:10.1016/s0142-9612(97)00223-8 · Cited by 406
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Muñoz, A. N. I., & Mischler, S. (2015) · Electrochimica Acta · doi:10.1016/j.electacta.2015.08.017 · Cited by 35
Liu, X., Miller, A. L., Xu, H., Waletzki, B. E., & Lu, L. (2019) · Biomacromolecules · doi:10.1021/acs.biomac.9b00133 · Cited by 35
AFM measurements of interactions between the platelet integrin receptor GPIIbIIIa and fibrinogen
Agnihotri, A., Soman, P., & Siedlecki, C. A. (2009) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2009.01.019 · Cited by 35
Self-citationNitric oxide releasing material adsorbs more fibrinogen
Lantvit, S. M., Barrett, B. J., & Reynolds, M. M. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34627 · Cited by 37
Lopes, F. S., de Oliveira, J. R., Milani, J., de Oliveira, L. D., Machado, J. P. B., Trava-Airoldi, V. J., Lobo, A. O., & Marciano, F. R. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.07.043 · Cited by 34
Silane coatings of metallic biomaterials for biomedical implants: A preliminary review
Somasundaram, S. (2018) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.34151 · Cited by 35
Wang, L., Li, G., Lin, Y., Zhang, Z., Chen, Z., & Wu, S. (2016) · Polymer Chemistry · doi:10.1039/c6py01043a · Cited by 33
Biocompatible superhydrophobic coating material for biomedical applications
Mahadik, S. A., Pedraza, F., Mahadik, S. S., Relekar, B. P., & Thorat, S. S. (2016) · Journal of Sol-Gel Science and Technology · doi:10.1007/s10971-016-4244-4 · Cited by 33
Latip, E. N. A., Coudron, L., McDonnell, M. B., Johnston, I., McCluskey, D., Day, R., & Tracey, M. C. (2017) · RSC Advances · doi:10.1039/c7ra10920b · Cited by 34
Anticoagulant Polyethylene Terephthalate Surface by Plasma-Mediated Fucoidan Immobilization
Özaltın, K., Lehocký, M., Humpolíček, P., Pelková, J., Martino, A. D., Karakurt, I., & Sáha, P. (2019) · Polymers · doi:10.3390/polym11050750 · Cited by 33
Pawłowski, Ł., Bartmański, M., Mielewczyk-Gryń, A. D., Cieślik, B. M., Gajowiec, G., & Zieliński, A. (2021) · Materials · doi:10.3390/ma14164533 · Cited by 33
Fukazawa, K., & Ishihara, K. (2013) · ACS Applied Materials & Interfaces · doi:10.1021/am402051e · Cited by 33
Advancements in Tissue Engineering: A Review of Bioprinting Techniques, Scaffolds, and Bioinks
Zoghi, S. (2024) · Biomedical Engineering and Computational Biology · doi:10.1177/11795972241288099 · Cited by 32
Lü, X., Zhang, H., Huang, Y., & Zhang, Y. (2018) · Regenerative Biomaterials · doi:10.1093/rb/rby017 · Cited by 32
Recent developments in the synthesis of poly(hydroxybutyrate) based biocomposites
Raza, Z. A., Noor, S., & Khalil, S. (2019) · Biotechnology Progress · doi:10.1002/btpr.2855 · Cited by 34
Movahedi, M., & Karbasi, S. (2023) · Journal of Polymers and the Environment · doi:10.1007/s10924-023-02800-6 · Cited by 32
Polymer Adhesion at the Solid–Liquid Interface Probed by a Single–Molecule Force Sensor
Geisler, M., Balzer, B. N., & Hugel, T. (2009) · Small · doi:10.1002/smll.200901237 · Cited by 34
Moraleda, B. F., Román, J. S., & Rodríguez-Lorenzo, L. M. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34528 · Cited by 32
Implications of wettability in biological materials science
Nychka, J. A., & Gentleman, M. M. (2010) · JOM · doi:10.1007/s11837-010-0107-6 · Cited by 32
Biocompatibility in hemodialysis: artificial membrane and human blood interactions
Ávila, E., Sepúlveda, R., Retamal, J., & Hachim, D. (2025) · BMC Nephrology · doi:10.1186/s12882-025-04401-y · Cited by 31
In vitro hemocompatibility of thin film nitinol in stenotic flow conditions
Kealey, C. P., Whelan, S. A., Chun, Y., Soojung, C. H., Tulloch, A. W., Mohanchandra, K. P., Carlo, D. D., Levi, D. S., Carman, G. P., & Rigberg, D. A. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.08.014 · Cited by 31
Electrically Active Materials for Medical Devices
Tofail, S. A. M., & Bauer, J. (2016) · IMPERIAL COLLEGE PRESS eBooks · doi:10.1142/p1090 · Cited by 31
Liu, R., Dai, J., Ma, L., Chen, J., Shi, X., Du, Y., Li, Z., & Deng, H. (2019) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2019.01.054 · Cited by 31
Atomic force microscope studies of fibrinogen adsorption
Averett, L. E., & Schoenfisch, M. H. (2010) · The Analyst · doi:10.1039/b924814e · Cited by 31
Ishihara, K., Mitera, K., Inoue, Y., & Fukazawa, K. (2020) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2020.111205 · Cited by 31
Enhancing the cell proliferation performance of NiTi substrate by laser diffusion nitriding
Ng, C., Rao, N., Law, W., Xu, G., Cheung, T.-L., Cheng, F. T., Wang, X., & Man, H. C. (2016) · Surface and Coatings Technology · doi:10.1016/j.surfcoat.2016.11.008 · Cited by 30
Augmenting endogenous repair of soft tissues with nanofibre scaffolds
Baldwin, M. J., Snelling, S. J. B., Dakin, S. G., & Carr, A. J. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2018.0019 · Cited by 30
Guindani, C., Dozoretz, P., de Araújo, P. H. H., Ferreira, S. R. S., & de Olíveira, D. (2018) · Materials Science and Engineering C · doi:10.1016/j.msec.2018.09.060 · Cited by 31
Srivas, P. K., Kapat, K., Das, B., Pal, P., Ray, P. G., & Dhara, S. (2019) · Applied Surface Science · doi:10.1016/j.apsusc.2019.02.039 · Cited by 30
Biomaterial Wettability Affects Fibrin Clot Structure and Fibrinolysis
Ruhoff, A. M., Hong, J. K., Gao, L., Singh, J., Tran, C., Mackie, G. M., & Waterhouse, A. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202100988 · Cited by 30
Sen, A., Barizuddin, S., Hossain, M., Polo‐Parada, L., Gillis, K. D., & Gangopadhyay, S. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2008.11.039 · Cited by 30
Liao, W., Lin, C., Wei, D., Shen, Y.-R., Li, Y.-C., Lee, J., & Liang, C. (2012) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34235 · Cited by 30
Shen, T., Yang, W., Shen, X., Chen, W., Tao, B., Yang, X., Yuan, J., Liu, P., & Cai, K. (2018) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.8b00791 · Cited by 30
Tulloch, A. W., Chun, Y., Levi, D. S., Mohanchandra, K. P., Carman, G. P., Lawrence, P. F., & Rigberg, D. A. (2010) · Journal of Surgical Research · doi:10.1016/j.jss.2010.01.014 · Cited by 29
Basiaga, M., Walke, W., Staszuk, M., Kajzer, W., Kajzer, A., & Nowińska, K. (2016) · Archives of Civil and Mechanical Engineering · doi:10.1016/j.acme.2016.08.001 · Cited by 29
Miyazaki, C. M., Mishra, R., Kinahan, D. J., Ferreira, M., & Ducrée, J. (2017) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2017.06.042 · Cited by 29
Mishra, S. K., Teotia, A. K., Kumar, A., & Kannan, S. (2016) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2016.08.010 · Cited by 29
Callaghan, N. I., Rempe, C. N., Froom, Z. S. C. S., Medd, K., & Huyer, L. D. (2024) · Materials Advances · doi:10.1039/d4ma00333k · Cited by 31
Kasoju, N., & Bora, U. (2010) · Advanced Engineering Materials · doi:10.1002/adem.200980055 · Cited by 28
Hynninen, V., Vuori, L., Hannula, M., Tapio, K., Lahtonen, K., Isoniemi, T., Lehtonen, E., Hirsimäki, M., Toppari, J. J., Valden, M., et al. (2016) · Scientific Reports · doi:10.1038/srep29324 · Cited by 28
Poly‐ L ‐lactide acid‐modified scaffolds for osteoinduction and osteoconduction
Bosetti, M., Fusaro, L., Nicolì, E., Borrone, A., Aprile, S., & Cannas, M. F. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.35016 · Cited by 28
Lai, Y., Chen, J., Zhang, T., Gu, D., Zhang, C., Li, Z., Lin, S., Fu, X., & Schultze–Mosgau, S. (2013) · Journal of Dentistry · doi:10.1016/j.jdent.2013.08.004 · Cited by 28
Engineered Microenvironments for Self-Renewal and Musculoskeletal Differentiation of Stem Cells
Hwang, Y., Phadke, A., & Varghese, S. (2011) · Regenerative Medicine · doi:10.2217/rme.11.38 · Cited by 28
Mukhopadhyay, S., Roy, S. S., D’Sa, R. A., Mathur, A. K., Holmes, R. J., & McLaughlin, J. A. (2011) · Nanoscale Research Letters · doi:10.1186/1556-276x-6-411 · Cited by 28
Kleinhans, C., Barz, J., Wurster, S., Willig, M., Oehr, C., Müller, M., Walles, H., Hirth, T., & Kluger, P. J. (2012) · Biotechnology Journal · doi:10.1002/biot.201200210 · Cited by 28
Aziz, G., Cools, P., Geyter, N. D., Declercq, H., Cornelissen, R., & Morent, R. (2015) · Biointerphases · doi:10.1116/1.4907755 · Cited by 28
Bera, T., Manna, I., & Majumdar, J. D. (2024) · Journal of Materials Processing Technology · doi:10.1016/j.jmatprotec.2024.118394 · Cited by 27
Kim, W.-J., Jang, C. H., & Kim, G. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.04.144 · Cited by 27
Segan, S., Jakobi, M., Khokhani, P., Klimosch, S. N., Billing, F., Schneider, M., Martin, D., Metzger, U., Biesemeier, A., Xiong, X. B., et al. (2020) · BioMed Research International · doi:10.1155/2020/3481549 · Cited by 28
Maciąg, F., Moskalewicz, T., Kowalski, K., Łukaszczyk, A., Hadzhieva, Z., & Boccaccini, A. R. (2021) · Materials · doi:10.3390/ma14020312 · Cited by 27
Kingman, J., & Dymond, M. K. (2022) · Chemical Data Collections · doi:10.1016/j.cdc.2022.100884 · Cited by 27
Physical and surface properties of polyurethane hydrogels in relation with their chemical structure
Sirkecioglu, A. N., Mutlu, H. B., Çıtak, C., Koc, A., & Güner, F. S. (2013) · Polymer Engineering and Science · doi:10.1002/pen.23640 · Cited by 27
Modeling and Experimental Validation of Microbial Transfer via Surface Touch
Zhao, P., & Li, Y. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c04678 · Cited by 26
Adhesion and proliferation of HeLa and fibroblast cells on chemically-modified gold surfaces
dos Santos, P. A., Rocha, C. D. S., & Baptista, M. S. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.09.034 · Cited by 26
Biomaterials: Characteristics and Properties
dos Santos, V., Brandalise, R. N., & Savaris, M. (2017) · Topics in mining, metallurgy and materials engineering · doi:10.1007/978-3-319-58607-6_2 · Cited by 26
Current advanced therapy cell-based medicinal products for type-1-diabetes treatment
Cañibano-Hernández, A., del Burgo, L. S., Espona‐Noguera, A., Ciriza, J., & Pedraz, J. L. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.03.041 · Cited by 26
Aghmiuni, A. I., Baei, M. S., Keshel, S. H., & Khiyavi, A. A. (2020) · Fibers and Polymers · doi:10.1007/s12221-020-9402-1 · Cited by 25
Sindhu, K. R., Bansode, N. D., Rémy, M., Morel, C., Bareille, R., Hagedorn, M., Hinz, B., Barthélémy, P., Chassande, O., & Boiziau, C. (2020) · Acta Biomaterialia · doi:10.1016/j.actbio.2020.08.012 · Cited by 26
Plasma mediated collagen‐I‐coating of metal implant materials to improve biocompatibility
Hauser, J., Köller, M., Bensch, S., Halfmann, H., Awakowicz, P., Steinau, H., & Esenwein, S. A. (2010) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.32672 · Cited by 25
Anderson, J. M. (2009) · Springer eBooks · doi:10.1007/978-0-387-98161-1_11 · Cited by 25
Özaltın, K., Lehocký, M., Humpolíček, P., Pelková, J., & Sáha, P. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060908 · Cited by 25
Mishra, G., Mittal, N., & Sharma, A. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b07831 · Cited by 25
Sharma, I., & Pattanayek, S. K. (2017) · Biophysical Chemistry · doi:10.1016/j.bpc.2017.03.011 · Cited by 25
Surface topography of polylactic acid nanofibrous mats: influence on blood compatibility
Soundararajan, A., Jyorthana Muralidhar, R., Dhandapani, R., Radhakrishnan, J., Manigandan, A., Kalyanasundaram, S., Sethuraman, S., & Subramanian, A. (2018) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-018-6153-2 · Cited by 25
Miyazaki, C. M., Camilo, D. E., Shimizu, F. M., & Ferreira, M. (2019) · Applied Surface Science · doi:10.1016/j.apsusc.2019.06.095 · Cited by 25
Boks, N. P., Kaper, H. J., Norde, W., Busscher, H. J., & van der Mei, H. C. (2008) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2008.08.021 · Cited by 25
Dickenson, M. E., Oakes, R. S., & Morris, A. H. (2026) · npj Biomedical Innovations. · doi:10.1038/s44385-025-00053-7 · Cited by 29
Li, X.-M., Li, H.-Z., Wang, S.-P., Huang, H.-M., Huang, H., Ai, H.-J., & Xu, J. (2014) · Materials Science and Engineering C · doi:10.1016/j.msec.2014.05.051 · Cited by 24
Atomic layer deposited ZnO films on stainless steel for biomedical applications
Basiaga, M., Walke, W., Kajzer, W., Sambok-Kiełbowicz, A., Szewczenko, J., Simka, W., Szindler, M., Ziębowicz, B., & Lubenets, V. I. (2020) · Archives of Civil and Mechanical Engineering · doi:10.1007/s43452-020-00148-5 · Cited by 24
Wang, R., Damanik, F., Kuhnt, T., Jaminon, A. M. G., Hafeez, S., Liu, H., Ippel, H., Dijkstra, P. J., Bouvy, N. D., Schurgers, L. J., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202202648 · Cited by 24
Senapati, S., Kaur, M., Singh, N., Kulkarni, S., & Singh, J. P. (2024) · ACS Applied Nano Materials · doi:10.1021/acsanm.4c00008 · Cited by 24
Huang, J., Wan, S., Liu, B., & Xue, Q. (2014) · Surface and Coatings Technology · doi:10.1016/j.surfcoat.2014.03.016 · Cited by 24
Lin, Z., Ma, Y., Zhao, C., Chen, R., Zhu, X., Zhang, L., Yan, X., & Yang, W. (2014) · Lab on a Chip · doi:10.1039/c4lc00223g · Cited by 25
On The Origin of Shear Stress Induced Myogenesis Using PMMA Based Lab-on-Chip
Naskar, S., Kumaran, V., & Basu, B. (2017) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.7b00206 · Cited by 24
Impact of formulation pH on physicochemical protein characteristics at the liquid-air interface
Koepf, E., Richert, M. E., Braunschweig, B., Schroeder, R., Brezesinski, G., & Frieß, W. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.02.009 · Cited by 24
Physics and Physiology of Cell Spreading in Two and Three Dimensions
Janmey, P. A., Hinz, B., & McCulloch, C. A. (2021) · Physiology · doi:10.1152/physiol.00020.2021 · Cited by 23
Bergara-Muguruza, L., Mäkelä, K. T., Yrjälä, T., Salonen, J. I., Yamashita, K., & Nakamura, M. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c14358 · Cited by 23
López-Ortega, A., de Viteri, V. S., Alves, S. A., Mendoza, G., Fuentes, E., Mitran, V., Cîmpean, A., Dan, I., Vela, A., & Bayon, R. (2022) · Biomaterials Advances · doi:10.1016/j.bioadv.2022.212875 · Cited by 23
Hybrid gold/graphene oxide reinforced polycaprolactone nanocomposite for biomedical applications
Joy, A., Unnikrishnan, G., Megha, M., Haris, M., Thomas, J. P., Kolanthai, E., & Senthilkumar, M. (2023) · Surfaces and Interfaces · doi:10.1016/j.surfin.2023.103000 · Cited by 24
Silva, J. P. D. S., Costa, R. C., NAGAY, B. E., Borges, M. H. R., Sacramento, C. M., da Cruz, N. C., Rangel, E. C., Fortulan, C. A., da Silva, J. H. D., Ruiz, K. G. S., et al. (2023) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.3c00491 · Cited by 23
Han, Z., Ostrikov, K., Tan, C. M., Tay, B. K., & Peel, S. A. F. (2011) · Nanotechnology · doi:10.1088/0957-4484/22/29/295712 · Cited by 23
Panda, N., Bissoyi, A., Pramanik, K., & Biswas, A. (2014) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2014.943548 · Cited by 23
Mechanisms of blood coagulation in response to biomaterials: Extrinsic factors
Kalathottukaren, M. T., & Kizhakkedathu, J. N. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-100497-5.00003-3 · Cited by 24
Thermoresponsive Stiffening with Microgel Particles in a Semiflexible Fibrin Network
Chaudhary, G., Ghosh, A., Bharadwaj, N. A., Kang, J. G., Braun, P. V., Schweizer, K. S., & Ewoldt, R. H. (2019) · Macromolecules · doi:10.1021/acs.macromol.9b00124 · Cited by 23
Alter macrophage adhesion and modulate their response on hydrophobically modified hydrogels
Xu, Z., Hwang, D., Bartlett, M. D., Jiang, S., & Bratlie, K. M. (2020) · Biochemical Engineering Journal · doi:10.1016/j.bej.2020.107821 · Cited by 24
Üstünel, Ş., Prévôt, M. E., Rohaley, G. A. R., Webb, C. R., Yavitt, B. M., Freychet, G., Zhernenkov, M., Pindak, R., Schaible, E. G., Zhu, C., et al. (2020) · Materials Advances · doi:10.1039/d0ma00676a · Cited by 24
Interfacial engineering for biomolecule immobilisation in microfluidic devices
Ashok, D., Singh, J., Howard, H. R., Cottam, S., Waterhouse, A., & Bilek, M. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.123014 · Cited by 22
Shirdar, M. R., Izman, S., Taheri, M. M., Assadian, M., & Kadir, M. R. A. (2015) · Arabian Journal for Science and Engineering · doi:10.1007/s13369-015-1611-3 · Cited by 22
Cell-Protein-Material Interaction in Tissue Engineering
Salmerón‐Sánchez, M., & Altankov, G. (2010) · InTech eBooks · doi:10.5772/8584 · Cited by 22
Yan, J., Xia, D., Xiong, P., Li, Y., Zhou, W., Li, Q., Wang, P., Zheng, Y., & Cheng, Y. (2020) · Journal of Material Science and Technology · doi:10.1016/j.jmst.2020.08.048 · Cited by 22
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Metadata
- Authors
- Xu, L.-C., & Siedlecki, C. A.
- Affiliations
- Pennsylvania State University (US)
- Corresponding author
- Siedlecki, Christopher A.
- Venue
- Biomaterials
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 28
- Issue
- 22
- Pages
- 3273-3283
- ISSN
- 0142-9612 (ISSN-L)
- PMC
- PMC3671914
- OpenAlex
- W1997848759
- Cited by
- 715
- References
- 53
- Citations by year
- 2026: 27 · 2025: 41 · 2024: 42 · 2023: 32 · 2022: 36 · 2021: 46 · 2020: 48 · 2019: 61 · 2018: 41 · 2017: 49 · 2016: 52 · 2015: 38 · 2014: 35 · 2013: 38 · 2012: 28
- FWCI
- 13.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biomaterials (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Pennsylvania Department of Health
- National Institutes of Health
- Huck Institutes of the Life Sciences
- National Heart, Lung, and Blood Institute (R01HL069965, R01 HL69965)
- Topics
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Surface Modification and Superhydrophobicity
- Keywords
- protein adsorption, protein adhesion, wettability, water contact angle, low-density polyethylene, contact time, bovine serum albumin, fibrinogen, biomaterial surfaces
- MeSH terms
- Tissue Adhesions, Adhesiveness, Biocompatible Materials, Blood Coagulation, Cell Adhesion, Fibrinogen, Humans, Protein Denaturation, Proteins, Surface Properties, Wettability, Microscopy, Atomic Force, Polyethylene
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