Biomimetics proteins

Ramsden J J 1998 Biomimetic protein immobilization using lipid bilayers Biosensors Bloelectronics 13 593—8... 

The unusual and interesting structural and spectroscopic properties of cupredoxin centers stimulated the synthesis of a number of biomimetic proteins (this section) and compounds (see Section 8.4.7). This research endeavor has contributed to the fundamental understanding of the role of each essential structural element in the formation of the cupredoxin center, in the display of its spectroscopic signatures, and in performance of its functions. It also helped to advance the field of metalloprotein design and engineering. Because of space limitation, only those model proteins and compounds that closely mimic the spectroscopic and/or structural properties of cupredoxin centers in their oxidized states (i.e., Cu for mononuclear and [Cu(1.5)---Cu(1.5)j for dinuclear centers) will be discussed in this chapter. 

Whittaker J, Balu R, Choudhury NR, Dutta NK (2014) Biomimetic protein-based elastomeric hydrogels for biomedical applications. Polym Int 63 1545-1557. doi 10.1002 1.4670... 

Artiflcial protein A Optimised IgG binding 22/8 Biomimetic protein L 8/7... 

Chiono V, Sirianni P, Bofflto M, Silvestri A, Sartori S, Gioffredi E, et al. Polyurethane scaffolds coated with biomimetic proteins for myocardial regeneration. J Tissue Eng Regen Med 2014 8 385-6. 

PARK are frequently used without surface modification. There are a significant number of papers and patents which describe PEEK modified with fillers such as hydroxyapatite (HA) or calcium phosphates, titanimn coatings or even biomimetic protein and peptide sequences. Some of these are described in reference [2]. However, in HA-filled PARK there is a trade-off between mechanical properties and modified biocompatibility. Various attempts have been made to overcome this limitation - for example by using HA coatings or HA whiskers [3, 4]. Biological modifications would be subject to extremely complex regulatory approval. In fact unmodified PEEK has been shown to be comparable in vitro with the bone forming capacity of titanium [5]. 

There is a clinical need for non-natural, functional mimics of the lung surfactant (LS) proteins B and C (SP-B and SP-C), which could be used in a biomimetic LS replacement to treat respiratory distress syndrome (RDS) in premature infants [56]. An effective surfactant replacement must meet the following performance requirements (i) rapid adsorption to the air-liquid interface, (ii) re-spreadabihty... 

In this chapter we describe the basic principles involved in the controlled production and modification of two-dimensional protein crystals. These are synthesized in nature as the outermost cell surface layer (S-layer) of prokaryotic organisms and have been successfully applied as basic building blocks in a biomolecular construction kit. Most importantly, the constituent subunits of the S-layer lattices have the capability to recrystallize into iso-porous closed monolayers in suspension, at liquid-surface interfaces, on lipid films, on liposomes, and on solid supports (e.g., silicon wafers, metals, and polymers). The self-assembled monomolecular lattices have been utilized for the immobilization of functional biomolecules in an ordered fashion and for their controlled confinement in defined areas of nanometer dimension. Thus, S-layers fulfill key requirements for the development of new supramolecular materials and enable the design of a broad spectrum of nanoscale devices, as required in molecular nanotechnology, nanobiotechnology, and biomimetics [1-3]. 

Most important for many applications of S-layer lattices in molecular nanotechnology, biotechnology, and biomimetics was the observation that S-layer proteins are capable of reassembling into large coherent monolayers on solid supports (e.g., silicon wafers, polymers, metals) at the air/water interface and on Langmuir lipid films (Fig. 6) (see Sections V and VIII). 

FIG. 14 Schematic illustration of an archaeal cell envelope structure (a) composed of the cytoplasmic membrane with associated and integral membrane proteins and an S-layer lattice, integrated into the cytoplasmic membrane, (b) Using this supramolecular construction principle, biomimetic membranes can be generated. The cytoplasmic membrane is replaced by a phospholipid or tetraether hpid monolayer, and bacterial S-layer proteins are crystallized to form a coherent lattice on the lipid film. Subsequently, integral model membrane proteins can be reconstituted in the composite S-layer-supported lipid membrane. (Modified from Ref. 124.)... 

In order to enhance the stability of hposomes and to provide a biocompatible outermost surface shucture for controlled immobihzation (see Section IV), isolated monomeric and oligomeric S-layer protein from B. coagulans E38/vl [118,123,143], B. sphaericus CCM 2177, and the SbsB from B. stearothermophilus PV72/p2 [119] have been crystallized into the respective lattice type on positively charged liposomes composed of DPPC, HD A, and cholesterol. Such S-layer-coated hposomes are spherical biomimetic structures (Fig. 18) that resemble archaeal ceUs (Fig. 14) or virus envelopes. The crystallization of S-... 

Knowledge about protein folding and conformation in biological systems can be used to mimic the design of a desired nanostructure conformation from a particular MBB and to predict the ultimate conformation of the nanostructure [152]. Such biomimetic nano-assembly is generally performed step by step. This wiU allow observation of the effect of each new MBB on the nanostructure. As a result, it is possible to control accurate formation of the desired nanostmcture. Biomimetic controlled and directed assembly can be utilized to investigate molecular interactions, molecular modeling, and study of relationships between the composition of MBBs and the final conformation of the nanostmctures. Immobilization of molecules on a surface could facilitate such studies [153]. 

Conventional MS in the energy domain has contributed a lot to the understanding of the electronic ground state of iron centers in proteins and biomimetic models ([55], and references therein). However, the vibrational properties of these centers, which are thought to be related to their biological function, are much less studied. This is partly due to the fact that the vibrational states of the iron centers are masked by the vibrational states of the protein backbone and thus techniques such as Resonance Raman- or IR-spectroscopy do not provide a clear picture of the vibrational properties of these centers. A special feature of NIS is that it directly reveals the fraction of kinetic energy due to the Fe motion in a particular vibrational mode. 

Cacia, J., Quan, C. P., Vasser, M., Sliwkowski, M. B., and Frenz, J., Protein sorting by high-performance liquid chromatography I. Biomimetic interaction chromatography of recombinant human deoxyribonuclease I on polyionic stationary phases, /. Chromatogr., 634, 229, 1993. 

Similarly to the above-mentioned entrapment of proteins by biomimetic routes, the sol-gel procedure is a useful method for the encapsulation of enzymes and other biological material due to the mild conditions required for the preparation of the silica networks [54,55]. The confinement of the enzyme in the pores of the silica matrix preserves its catalytic activity, since it prevents irreversible structural deformations in the biomolecule. The silica matrix may exert a protective effect against enzyme denaturation even under harsh conditions, as recently reported by Frenkel-Mullerad and Avnir [56] for physically trapped phosphatase enzymes within silica matrices (Figure 1.3). A wide number of organoalkoxy- and alkoxy-silanes have been employed for this purpose, as extensively reviewed by Gill and Ballesteros [57], and the resulting materials have been applied in the construction of optical and electrochemical biosensor devices. Optimization of the sol-gel process is required to prevent denaturation of encapsulated enzymes. Alcohol released during the... 

Wong, K.K.W., Douglas, T Gider, S Awschalon, D.D. and Mann, S. (1998) Biomimetic synthesis and characterization of magnetic proteins (magnetoferritin). Chemistry of Materials, 10, 279-285. 

Leonor, I.B., Azevedo, H.S., Alves, C.M. and Reis, R.L. (2003) Effects of the incorporation of proteins and active enzymes on biomimetic caldum-phosphate coatings. Key Engineering Materials, 240-242, 97—100. 

Abstract Protein-like copolymers were first predicted by computer-aided biomimetic design. These copolymers consist of comonomer units of differing hydrophilicity/hydro-phobicity. Heterogeneous blockiness, inherent in such copolymers, promotes chain folding with the formation of specific spatial packing a dense core consisting of hydrophobic units and a polar shell formed by hydrophilic units. This review discusses the approaches, those that have already been described and potential approaches to the chemical synthesis of protein-like copolymers. These approaches are based on the use of macromolecular precursors as well as the appropriate monomers. In addition, some specific physicochemical properties of protein like copolymers, especially their solution behaviour in aqueous media, are considered. 

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