Cell adhesion on a polymerized peptide-amphiphile monolayer

被引:62
作者
Biesalski, MA [1 ]
Knaebel, A
Tu, R
Tirrell, M
机构
[1] Univ Calif Santa Barbara, Dept Chem Engn, Mat Res Lab, Santa Barbara, CA 93106 USA
[2] Univ Calif Santa Barbara, Inst Collaborat Biotechnol, Santa Barbara, CA 93106 USA
基金
美国国家科学基金会;
关键词
RGD peptide; cell adhesion polymerization; Langmuir-Blodgett film;
D O I
10.1016/j.biomaterials.2005.08.002
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
We report the synthesis and characterization of a stable polymerized monolayer of peptide-amphihiles on a planar solid Support that promotes mouse fibroblast cell adhesion and spreading. Peptide-amphiphiles consisting of a polymerizable fatty acid attached to a short RGD containing peptide sequence are self-assembled and polymerized at the water-air interface by means of the Langmuir-Blodgett technique. The surface concentration of the peptide-amphiphile is varied by co-spreading the peptide-amphiphile with an analogous non-modified polymerizable amphiphile at the water/air interface, prior to UV light-induced polymerization. The polymerized monolayer is transferred onto a hydrophobized smooth mica surface and the resulting surfaces have been investigated with respect to directing the cell adhesion and spreading of mouse fibroblast cells in a serum-free medium. Fibroblast cells adhere and spread on surfaces exposing the bioactive ligand but do not spread on reference surfaces Without peptide. We find a maximum number of adherent cells at rather high peptide surface concentrations of about 10 mol% in the mixed monolayer, equivalent to more than 50 pmol/cm(2) peptide on the surface of the film. We attribute this finding to a limited accessibility of the ligands by the integrins. Because of the stability of the polymerized peptide-amphiphile monolayer, these surfaces can be re-seeded multiple times with cells, i.e. adherent cells can be removed from the surface, the surface can be sterilized and cells can be re-attached. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1259 / 1269
页数:11
相关论文
共 39 条
[1]   Activation of integrin function by nanopatterned adhesive interfaces [J].
Arnold, M ;
Cavalcanti-Adam, EA ;
Glass, R ;
Blümmel, J ;
Eck, W ;
Kantlehner, M ;
Kessler, H ;
Spatz, JP .
CHEMPHYSCHEM, 2004, 5 (03) :383-388
[2]   Differential modulation of human melanoma cell metalloproteinase expression by α2β1 integrin and CD44 triple-helical ligands derived from type IV collagen [J].
Baronas-Lowell, D ;
Lauer-Fields, JL ;
Borgia, JA ;
Sferrazza, GF ;
Al-Ghoul, M ;
Minond, D ;
Fields, GB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (42) :43503-43513
[3]   Induction of endothelial cell activation by a triple helical α2β1 integrin ligand, derived from type I collagen α1(I)496-507 [J].
Baronas-Lowell, D ;
Lauer-Fields, JL ;
Fields, GB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (02) :952-962
[4]  
BEER JH, 1992, BLOOD, V79, P117
[5]   SYNTHETIC LIPIDATION OF PEPTIDES AND AMINO-ACIDS - MONOLAYER STRUCTURE AND PROPERTIES [J].
BERNDT, P ;
FIELDS, GB ;
TIRRELL, M .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (37) :9515-9522
[6]  
Biesalski M, 2005, LANGMUIR, V21, P5663, DOI 10.1021/la0504558
[7]   Biomedical surface science: Foundations to frontiers [J].
Castner, DG ;
Ratner, BD .
SURFACE SCIENCE, 2002, 500 (1-3) :28-60
[8]   DIRECT COLORIMETRIC DETECTION OF A RECEPTOR-LIGAND INTERACTION BY A POLYMERIZED BILAYER ASSEMBLY [J].
CHARYCH, DH ;
NAGY, JO ;
SPEVAK, W ;
BEDNARSKI, MD .
SCIENCE, 1993, 261 (5121) :585-588
[9]   Targeted cellular adhesion at biomaterial interfaces [J].
Dillow, AK ;
Tirrell, M .
CURRENT OPINION IN SOLID STATE & MATERIALS SCIENCE, 1998, 3 (03) :252-259
[10]  
Dori Y, 2000, J BIOMED MATER RES, V50, P75, DOI 10.1002/(SICI)1097-4636(200004)50:1<75::AID-JBM11>3.0.CO