Evidence map›Paper›PMID 17466368›Full record

ArticleBiomaterials2007

Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces.

Li-Chong Xu, Christopher A Siedlecki

Abstract read
In one paragraph

Article in Biomaterials, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
15.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 701 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. PVP-Stabilized Ag@SiOInternational journal of nanomedicine · 2026
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  11. Article
  12. Review
  13. Review
  14. Surface engineeringChemical engineering journal (Lausanne, Switzerland : 1996) · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Incorporation of Poly(propylene succinate-ACS applied bio materials · 2025
    Article
  20. Article

80 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Li-Chong XuDepartment of Surgery, Biomedical Engineering Institute, The Pennsylvania State University, College of Medicine, Hershey, PA 17033, USA.
Christopher A Siedlecki
Pennsylvania State University · US

Funding

SURFACE ENGINEERING IN CONTACT ACTIVATION OF COAGULATIONR01HL069965 · NHLBI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI SIEDLECKI, CHRISTOPHER A · 2002 to 2014
$4.1M
NHLBI NIH HHS R01 HL069965NHLBI NIH HHS R01 HL69965
6 · The paper itself

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.

Indexed as

Surface PropertiesAdhesivenessBiocompatible MaterialsBlood CoagulationCell AdhesionFibrinogenHumansMicroscopy, Atomic ForcePolyethyleneProtein DenaturationProteinsTissue AdhesionsWettabilityBiocompatible MaterialsFibrinogenPolyethyleneProteins

Identifiers

PMID17466368
PMCPMC3671914
OpenAlexW1997848759

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.