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Modification of glassy carbon surfaces with synthetic laminin-derived peptides for nerve cell attachment and neurite growth.

作者信息

Huber M, Heiduschka P, Kienle S, Pavlidis C, Mack J, Walk T, Jung G, Thanos S

机构信息

University of Münster, Eye Hospital, Germany.

出版信息

J Biomed Mater Res. 1998 Aug;41(2):278-88. doi: 10.1002/(sici)1097-4636(199808)41:2<278::aid-jbm13>3.0.co;2-h.

Abstract

Interactions between cultured nerve cells and surfaces are of importance for the implantation of biocompatible electrode materials such as glassy carbon (GC). Since implants serve as recording sensors in prosthetic neuroscience, we investigated whether coating electrodes with certain laminin derivatives containing the peptide sequences SIKVAV, CDPGYIGSR, PDSGR, YFQRYLI, and RNIAEIIKDA influences neuronal adhesion and neurite outgrowth in vitro. The coating of GC was performed by electrochemical polymerization and, for comparison, by adsorption or covalent coupling. Electrochemical polymerization is suitable for the coupling of peptides to GC, as shown by amino acid analysis and sequencing. Embryonic chicken retinal ganglion cells and brain cells (days E7 or E17) were used for both attachment and growth studies. Surfaces made by electrochemical polymerization of peptides were more efficient than those made by adsorption or covalent coupling of peptides. Synthetic cyclic peptide derivatives of CDPGYIGSR and 18-mer SIKVAV were found to be more efficient than the linear peptides. Competitive effects that resulted in a decreased cell attachment could be found upon application of soluble peptides. Nevertheless, irrespective of the method of coating, peptides were less efficient compared with the whole laminin molecule, as expected from its multiple adhesion sites. When small GC pins were implanted into the brain of E17 chicken after coating with the 18-mer SIKVAV peptide, nerve cell attachment was observed in vivo. The results suggest that chronically implantable materials may exert a higher neurocompatibility when coated with synthetic peptides.

摘要

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