Understanding endothelialization: Rate limitations in chemotaxis

William H. Velander, Cicely Washington

Research output: Contribution to conferencePaperpeer-review


Physiological wound healing is a process that consists of a highly orchestrated sequence of events stimulated by various growth factors. The biological half-lives of growth factors are short so in order to apply them therapeutically they must be delivered in an efficient manner. Immobilization of growth factors at the target site may potentially enhance their effect. A 43.3-kDa collagen-binding fusion protein (CBDR136K) consisting of both R136K, FGF-1 with the Arginine at the 136 site changed to Lysine via site directed mutagenesis, and a collagen binding domain derived from Clostridium histolyticum collagenase was produced. The changes to FGF-1 do not alter its mitogenic nor chemotactic response to HUVEc or NIH 3T3 cells. In the presence of thrombin R136K and CBDR136K maintain their chemotactic properties while that of FGF-1 is reduced by a half. Surface plasmon resonance biosensing was used to quantify binding interactions to a soluble synthetic collagen peptide analog. The binding affinity constant to a KW(POG)8 peptide with FGF-1, R136K, CED, CBDR136K were 5.1 × 10-6 M, 3.4 × 10-6 M, 0.89 × 10-8 M, and 1.1 × 10-8 M respectively. Because the CBDR136K retains its mitogenic potential, it may be feasible to use it or similar chimeric proteins to immobilize growth factors at the site of damaged tissue and increase efficiency of endothelialization of wound sites or acellular, collagenous surfaces.

Original languageEnglish (US)
Number of pages1
StatePublished - 2005
Externally publishedYes
Event05AIChE: 2005 AIChE Annual Meeting and Fall Showcase - Cincinnati, OH, United States
Duration: Oct 30 2005Nov 4 2005


Conference05AIChE: 2005 AIChE Annual Meeting and Fall Showcase
Country/TerritoryUnited States
CityCincinnati, OH

ASJC Scopus subject areas

  • Engineering(all)


Dive into the research topics of 'Understanding endothelialization: Rate limitations in chemotaxis'. Together they form a unique fingerprint.

Cite this