Cited by 715Polymer Surface Interaction StudiesForce Microscopy Techniques and ApplicationsSurface Modification and Superhydrophobicity

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

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Abstract

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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Crossref · 10.1016/j.biomaterials.2007.03.032

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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)
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
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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