Recognition of Protein Surfaces

Similarly, this amphiphilic polymer micelle was also used to dismpt the complex between cytochrome c (Cc) and cytochrome c peroxidase (CcP Sandanaraj, Bayraktar et al. 2007). In this case, we found that the polymer modulates the redox properties of the protein upon binding. The polymer binding exposes the heme cofactor of the protein, which is buried in the protein and alters the coordination environment of the metal. The exposure of heme was confirmed by UV-vis, CD spectroscopy, fluorescence spectroscopy, and electrochemical kinetic smdies. The rate constant of electron transfer (fc°) increased by 3 orders of magnimde for the protein-polymer complex compared to protein alone. To establish that the polymer micelle is capable of disrupting the Cc-CcP complex, the polymer micelle was added to the preformed Cc-CcP complex. The observed for this complex was the same as that of the Cc-polymer complex, which confirms that the polymer micelle is indeed capable of disrupting the Cc-CcP complex. 

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Hamuro, Yoshimoto, Hamilton, Andrew D., Calama, Mercedes Crego, Park, Hyung Soon. 1997., "A Calixarene with Four Peptide Loops An Antibody Mimic for Recognition of Protein Surfaces." Angewandte Chemie, International English Edition, 36(23) 2680-2683. 

Rutledge SE, Volkman HM, Schepartz A (2003) Molecular recognition of protein surfaces high affinity ligands for the CBPKIX domain. J Am Chem Soc 125 14336-14347... 

On the contrary, recognition processes occurring at the surface of proteins are more difficult to confiol due to the large featureless shape (about 750-1500 A) and the highly solvated area of contact. Thus, recognition of protein surfaces requires multivalency and cooperative effects to achieve high binding constants and selectivity for specific proteins. ... 

On the basis of these results, the Schrader group decided to exploit the selective binding properties of their diphos-phonate anions for the recognition of protein surfaces. Host... 

CT-induced colorization of solutions of an aromatic peptide as a result of their encapsulation by coordination capsule 486 (Scheme 6.6) is reported in [9] to be applicable for the naked-eye recognition of three aromatic residues (Trp, Tyr, and Phe) the selectivity of this binding may be used for site-specific recognition of protein surfaces. 

Molecular recognition and binding is the first step in protein electron-electron transfer. The foregoing data suggests that for the prototypical cyt c ccp system, this binding does not involve specific lock and key recognition, but rather involves complementary sticky patches of protein surfaces (rather like two pieces of velcro adhesive). 

We need to have drugs, antidotes, and cures for the weapons of mass destruction that terrorists are likely to use. To develop medicinal countermeasures, the basic science involved must first be understood. For both chemical and biological weapons, the process of molecular recognition by elements of the human body is of utmost importance. However, we do not have a clear understanding of protein surface interactions, the relationship of genes to protein function, and how viruses infect and replicate. All of these processes are chemical in nature and caimot be solved without knowledge of the chemical sciences. 

Home WS, Johnson LM, Ketas TJ et al (2009) Structural and biological mimicry of protein surface recognition by a/P-peptide foldamers. Proc Natl Acad Sci USA 106 14751-14756... 

H.Q., Shi Ratner, B.D. Template recognition of protein-imprinted polymer surfaces. J. Biomed. Mater. Res. Part A 2000, 49, 1. 

There has been work by various groups devoted to this surface imprinting [63-72]. Silica [63-65] and polymer [66,71] particles had been modified, so that polymerizable groups were available which could react during a homogeneously initiated polymerization (see Scheme 4a). Particles had been imprinted also for the recognition of proteins [67,68]. 

Biocompatibility of materials— biomaterials —in contact with cells or tissue, relies on specific molecular recognition processes, especially at the interfaces. Imprinted surfaces are expected to play a key role in this field in the future [114]. Ultrathin or thin MIP layers for recognition of proteins, but also for cell-specific recognition based on surface-marker structures or cell shape could be envisioned. 

We can also mention the use of bio-sourced building blocks based on cellulose or dextran. Kadla et al. described value-added materials from naturally abundant polymers for system that may serve as a platform for the design and development of biosensors [197]. A hierarchically strucmred honeycomb film from dextran-ft-PS amphiphilic linear diblock copolymers has also been described by Chen et al. leading to ordered porous bio-hybrid films. [198] Honeycomb patterned surfaces functionalized with biomolecules for specific recognition of proteins or bacteria have been also achieved either by self-assembly of amphiphilic copolymers based on galactose moieties [155] or by post-modification with peptide sequences [199]. 

Equally, stabilizing protein-protein interactions has considerable therapeutic potential. For instance, p53 is an important cell cycle protein involved in programmed cell death (apoptosis), which associates to form a tetramer in vivo Furthermore, p53 mutations are commonplace in a wide variety of cancers.Giralt et al. have investigated the development of protein surface recognition sequences that are rich in positively charged residues and bind to anionic domains in monomeric p53 and concluded that such an approach offers considerable potential for targeting the cell cycle in cancerous cells. 

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