Adhesion domains

Sacca, B., Fiori, S., and Moroder, L. (2003). Studies of the local conformational properties of the cell-adhesion domain of collagen type IV in synthetic heterotri-meric peptides. Biochemistry 42, 3429-3436. 

Specific domains of proteins (for example, those mentioned in the section Organic Phase ) adsorbed to biomaterial surfaces interact with select cell membrane receptors (Fig. 8) accessibility of adhesive domains (such as specific amino acid sequences) of select adsorbed proteins may either enhance or inhibit subsequent cell (such as osteoblast) attachment (Schakenraad, 1996). Several studies have provided evidence that properties (such as chemistry, charge, and topography) of biomaterial surfaces dictate select interactions (such as type, concentration, and conformation or bioactivity) of plasma proteins (Sinha and Tuan, 1996 Horbett, 1993 Horbett, 1996 Brunette, 1988 Davies, 1988 Luck et al., 1998 Curtis and Wilkinson, 1997). Albumin has been the protein of choice in protein-adsorption investigations because of availability, low cost (compared to other proteins contained in serum), and, most importantly, well-documented conformation or bioactive structure (Horbett, 1993) recently, however, a number of research groups have started to examine protein (such as fibronectin and vitronectin) interactions with material surfaces that are more pertinent to subsequent cell adhesion (Luck et al., 1998 Degasne et al., 1999 Dalton et al., 1995 Lopes et al., 1999). 

Fig. 8. Schematic representation of protein-mediated cell adhesion on biomaterial surfaces. Biomaterial surface properties (such as hydrophilicity/hydrophobicity, topography, energy, and charge) affect subsequent interactions of adsorbed proteins these interactions include but are not limited to adsorbed protein type, concentration, and conformation. Changes in protein-surface interactions may alter accessibility of adhesive domains (such as the peptide sequence arginine-glycine-aspartic acid) to cells (such as osteoblasts, fibroblasts, or endothelial cells) and thus modulate cellular adhesion. (Adapted and redrawn from Schakenraad, 1996.)...

Wyss DF, et al. Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science 1995 269 1273-1278. 

Action patterns Adhesion domains Affinity and mechanism-based inhibitors Catalytic domains Classification schemes Hydrolases Lyases Mechanism of action Phosphorylases Proteinaceous inhibitors... 

The partial NMR spectroscopic studies of intact glycoproteins so far reported, indicates that the core Gn of N-glycan at amino-terminal adhesion domain... 

On the nanoscale, the surface chemistry of the scaffold must recreate the important cell-ECM properties of adhesion and control. Biocompatibility of the scaffold surface with cells is key for allowing adhesion and migration of cells. The amino acid sequence of arginine-glycine-aspartic acid (RGD) has been identified on fibronectin and other ECM glycoproteins as a key adhesion domain, and the design of synthetic scaffolds incorporating the peptide has been successful... 

Domains L homology domain Ig immunoglobulin-like domain SAM sterile alpha motif Cadherin cell-cell adhesion domain Explanations to some of the receptors PDCFR platelet derived growth fac-... 

PfEMPl is an adhesive and antigenic molecule (Kraemer and Smith, 2006 Kyes et al., 2001, 2007 Smith et al., 2000a) composed of three different adhesive domains DBL, CIDR and a constant domain C2. The extracellular portion of PfEMPl variants contains between two and seven cysteine-rich DBL domains and each can be divided into 10 semi-conserved blocks (A-J) and 10 variable blocks (1-10) (Howell et al.,... 

Smith, J. D., Subramanian, G., Gamain, B., Baruch, D. I., and Miller, L. H. (2000a). Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family. Mol. Biochem. Parasitol. 110,293-310. 

These studies suggest a novel pathway in which heterotrimeric G-protein signaling controls proper localization and function of SJ proteins at the pericardial adhesion domain of CBs, which leads to the establishment of stable "SJ-like" adhesive contacts with pericardial cells to maintain the mature dorsal vessel lumen. 

A more recent example of a biotransformation of peptide-polymer conjugates combines biocombinatorial procedures with enzjonatic activation processes in order to realize mussel-glue inspired adhesion. Phage-display biopanning incorporating tyrosinase to transform L-tyrosine residues to L-dopa enabled the direct selection of enzymatically activable 12-mer peptide adhesion domains for aluminum oxide (Figure 1.21). 

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