RGD-containing proteins

ADAMs are membrane proteins that contain a disintegrin and a metalloprotease domain. Disintegrins are RGD-containing proteins that inhibit cell/matrix interactions (adhesion) and cell/cell interactions (aggregation) through the integrin receptors. In addition, ADAMs have two other domains that are involved in signaling and transport (113). 

Collins WED, Mosher F, Tomasini Br, Cooper SL A preliminary comparison of the thrombogenic activity of vitronectin and other RGD-containing proteins when bound to surfaces. Aim N Y Acad Sci 516 291-292,1988. 

S.H. Hsu, S.W. Whu, S.C. Hsidi, C.L. Tsai, D.C. Chen, T.S. Tan, Evaluation of chitosan-alginate—hyaluronate complexes modified by an RGD-containing protein as tissue-engineering scaffolds for cartilage regenaation, Artif. Organs 28 (2004) 693—703. 

Helfrich MH, Nesbitt SA, Dorey EL, Horton MA (1992) Rat osteoclasts adhere to a wide range of RGD (Arg-Gly-Asp) peptide-containing proteins, including the bone sialoproteins and fibronectin, via a beta 3 integrin. J Bone Miner Res 7 335-343... 

In an alternative scenario, 7-mer or 20-mer oligolysine sequences (which interact with heparan sulfate) have been fused to the C terminus of the fiber protein. This modification led to a dramatically increased and CAR-independent transduction of endothelial cells, smooth muscle cells, and macrophages in vitro and in vivo (up to > 100-fold) [33, 34], of myeloma cells and AML blast cells in vitro [35, 36], and of cultured glioma cells in vitro [37, 38], A similar approach has been used to fuse an RGD peptide (RDG-4C) to the C terminus of the fiber, which led to an increased transduction of endothelial cells in vitro and in vivo [33, 39], The same RGD-containing peptide has also been incorporated into the HI-loop of the fiber protein, resulting in an up to 1000-fold increased and CAR-independent transduction of primary endothelial cells and ovarian and head and neck cancer cells in vitro [40, 41]. 

For this review we have selected the cyclic modified peptides mentioned above, i.e. vancomycin, nisin, cyclosporin, and cyclotheonamide, as well as two examples, i.e. RGD-containing cyclic peptides and SH2 domain binding cyclic peptides, which were inspired by proteins. 

More productive chemical results, which stiU harness the destructive action of ultrasound on certain bonds, can be attained when sonication is applied to biological fluids (e.g. protein solutions) en route to bionanomaterials [15], A conspicuous example can be found in sonochemically-prepared protein microspheres, in which the interplay of mechanical effects (emulsification) and chemical effects (formatiOT of transient species) is noticeable. A protein emulsion is readily created at the interface between two immiscible liquid phases, while radicals generated by water sonolysis promote disulfide bond cross-linking between cysteine residues. Surface modifications, via conjugation with monoclonal antibodies or RGD-containing peptides, can also be carried out [102, 103]. The sonochemical preparation of chitosan microspheres also exploits the intermolecular cross-linking of imine bonds from the sugar precursor [104]. 

The amino acid sequence ROD (Arg-Gly-Asp) is present in many extracellular matrix (ECM) proteins and has been found to play an important role in cellular growth, differentiation, proliferation, and regulation of overall cell function. Immobilized, synthetic, RGD-containing peptides on solid supports such as polymers and silicon oxide surfaces have been reported to mediate specific surface-cell interactions and to promote cell organization. Studies of cell migration suggest the importance of the surface density of RGD sequences for efficient cell-matrix in-teraction. ... 

ALA Aminolevulinic acid, GC glycolchitosan, FAK focal adhesion kinase, IL-12 interleukin-12, PDTC pyrrolidinedithiocarbamate, PLXDCl plexin domain-containing protein 1, POSTN periostin, RGD Arg-Gly-Asp peptide, siRNA short interfering RNA... 

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