期刊
ADVANCED DRUG DELIVERY REVIEWS
卷 62, 期 15, 页码 1404-1455出版社
ELSEVIER
DOI: 10.1016/j.addr.2010.07.001
关键词
Elastic-contractile model proteins; Gibbs free energy(hydrophobic association); Elasticity of (GVGVP)(n); Multi-drug resistance (MDR); Drug-laden nanoparticles; Antigen binding fragments Fab1/Fab2
资金
- Bioelastics Inc.
- Polish Ministry of Science and Higher Education [0172/B/P01/2009/36]
This review presents the structure and physico-chemical properties of ECMPs, elastic-contractile model proteins using sparse design modifications of elastic (GVGVP)(n); it describes the capacity of ECMP to perform the energy conversions that sustain living organisms; it arrives at the hydration thermodynamics of ECMP in terms of the change in Gibbs free energy of hydrophobic association, Delta G(HA), and the apolar-polar repulsive free energy of hydration. Delta G(ap); it applies Delta G(HA), Delta G(ap), and the nature of elasticity to describe the function of basic diverse proteins, namely - the F-1-motor of ATP synthase, Complex III of mitochondria, the KscA potassium-channel, and the molecular chaperonin, GroEL/ES; it applies Delta G(HA) and Delta G(ap), to describe the function of ABC exporter proteins that confer multi-drug resistance (MDR) on micro-organisms and human carcinomas and suggests drug modifications with which to overcome MDR. Using ECMP, means are demonstrated, for quantifying drug hydrophobicity with which to combat MDR and for preparing ECMP drug delivery nanoparticles, ECMPddnp, decorated with synthetic antigen-binding fragments, Fab1 and Fab2, with which to target specific up-regulated receptors, characteristic of human carcinoma cells, for binding and localized drug release. (C) 2010 Elsevier B.V. All rights reserved.
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