Design and function of novel osteoblast-adhesive peptides for chemical modification of biomaterials

✍ Scribed by Dee, Kay C. ;Andersen, Thomas T. ;Bizios, Rena

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 168 KB
• Volume: 40
• Category: Article
• ISSN: 0021-9304
• DOI: 10.1002/(sici)1097-4636(19980605)40:3<371::aid-jbm5>3.0.co;2-c

✦ Synopsis

Proactive, ''next generation'' dental/orthopedic biomaterials must be designed rationally to elicit specific, timely, and desirable responses from surrounding cells/ tissues; for example, such biomaterials should support and enhance osteoblast adhesion (a crucial function for anchorage-dependent cells). In the past, integrin-binding peptides have been immobilized on substrates to partially control osteoblast adhesion; the present study focused on the design, synthesis, and bioactivity of the novel peptide sequence Lys-Arg-Ser-Arg that selectively enhances heparan sulfatemediated osteoblast adhesion mechanisms. Osteoblast, but not endothelial cell or fibroblast, adhesion was enhanced significantly (p < 0.05) on substrates modified with Lys-Arg-Ser-Arg peptides, indicating that these peptides may be osteoblast-or bone cell specific. Blocking osteoblast cellmembrane receptors with various concentrations of soluble Arg-Gly-Asp-Ser peptides did not inhibit subsequent cell adhesion on substrates modified with Lys-Arg-Ser-Arg peptides, providing evidence that osteoblasts interact with Arg-Gly-Asp-Ser and with Lys-Arg-Ser-Arg peptides via distinct (i.e., integrin-and proteoglycan-mediated) mechanisms, each uniquely necessary for osteoblast adhesion. The present study constitutes an example of rational design/ selection of bioactive peptides, confirms that osteoblast adhesion to substrates can be controlled selectively and significantly by immobilized peptides, and elucidates criteria and strategies for the design of proactive dental/orthopedic implant biomaterials.