Peptide-PEG Amphiphiles as Cytophobic Coatings for Mammalian and Bacterial Cells

Abstract

Amphiphilic macromolecules containing a polystyrene-adherent peptide domain and a cell-repellent poly(ethylene glycol) domain were designed, synthesized, and evaluated as a cytophobic surface coating. Such cytophobic, or cell-repellent, coatings are of interest for varied medical and biotechnological applications. The composition of the polystyrene binding peptide domain was identified using an M13 phage display library. ELISA and atomic force spectroscopy were used to evaluate the binding affinity of the amphiphile peptide domain to polystyrene. When coated onto polystyrene, the amphiphile reduced cell adhesion of two distinct mammalian cell lines and pathogenic Staphylococcus aureus strains.

Peptide Interfacial Biomaterials Improve Endothelial Cell Adhesion and Spreading on Synthetic Polyglycolic Acid Materials

“…27 We have also previously reported peptides that bind metals, metal oxides, and plastics. 23,34,54 Both Sanghvi et al and Meyer et al individually described bimodular RGD peptides that promoted cell adhesion to polypyrrole and Ti metal, respectively. 34,46,47 Application of IFBMs to degradable biomaterials such as PGA has not been previously reported.…”

“…In this fashion, these peptides create an interface that allows for appropriate biological interactions with inert materials. Our previous research focused on using bifunctional resulting peptides to regulate the interactions that occurred at the biological-material interface including: promotion of surface cellularization, 34 suppression of apoptosis, 36 prevention of fouling, 23,24 and, more recently, release of a therapeutic from a surface. 35 In this report, we have approached the problem of poor biological activity of PGA fibers by developing a modular IFBM peptide that is capable of binding to PGA and modifying its surface to provide biological cues that direct endothelial cell adhesion, spreading, cytoskeletal reorganization, and focal adhesion plaque formation.…”

“…23,24,[34][35][36]54 These bifunctional, two-domain peptide coatings must recognize and bind both the inert surface through non-covalent physisorption, while also providing a mechanism to interact with the surrounding biology. In this fashion, these peptides create an interface that allows for appropriate biological interactions with inert materials.…”

Directed self‐immobilization of alkaline phosphatase on micro‐patterned substrates via genetically fused metal‐binding peptide

“…During the last decade, combinatorial biology libraries have been employed for selection of inorganic binding peptides which are utilized as biosynthesizers, molecular linkers, and assemblers (Brown et al, 2000;Kramer et al, 2004;Kriplani and Kay, 2005;Sano et al, 2005;Sarikaya et al, 2003;Whaley et al, 2000). Furthermore, solid-binding peptides were also selected for synthetic polymeric materials (Adey et al, 1995;Kenan et al, 2006). Molecular biology protocols further allow tailoring of the selected peptides to tune their binding and materialselective properties so that they can be used in bionanotechnological applications, such as linkers for solid colloidal nanoparticles and flat substrates (e.g., gold or glass) (Kacar et al, 2009;Tamerler et al, 2006a).…”

Staphylococcus aureus resistance on titanium coated with multivalent PEGylated-peptides

“…Hence, we turn to bio-adhesives and take advantage of the natural affinity of peptides and proteins for synthetic materials in the development of more versatile anchors for the PEGylation of implant materials. Increasingly, engineered polypeptides capable of recognizing synthetic materials are being investigated for use as adhesive moieties to immobilize various functionalities on surfaces [22-26]. This strategy also allows for rapid and facile modification of surfaces without the need for harsh reaction conditions, and is therefore amenable to simple, point-of-care application in a surgical setting.…”