The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
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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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
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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
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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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