Characterization, Stability, and Formulations of Basic Fibroblast Growth Factor

Wang, Y J; Shahrokh, Zahra; Vemuri, Sriram; Eberlein, Gert; Beylin, I; Busch, Michelle

doi:10.1007/0-306-47452-2_2

Cited by 24 publications

(27 citation statements)

References 47 publications

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“…Although many buffering agents are available for pH adjustment, the aggregation behavior of proteins can be signifi cantly different in different buffer systems. 43,106,170,171 Phosphate buffers have been shown to have a negative effect on protein aggregation in several studies. Katayama et al 31 studied the effects of buffering species on the aggregation of IFN -tau at pH 7 at 50 ° C and found that the protein aggregation rate was fastest in phosphate buffer, slower in Tris buffer, and slowest in histidine buffer.…”

Section: Type and Concentration Of Buffering Agentsmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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Section: Type and Concentration Of Buffering Agentsmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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“…FGF-2 is widely used to accelerate wound healing 28,29) . FGF-2 promotes the proliferation of various types of cells such as vascular endothelial cells, chondrocytes, osteoblasts, and mesenchymal stem cells [30][31][32][33] .…”

Section: Loading and Release Of Fibroblast Growth Factor-2 (Fgf-2)mentioning

confidence: 99%

“…This is probably because of the difference in the molecular size of BSA and FGF-2. The size of FGF-2 and BSA are 17 and 67 kDa, respectively, and the average diameter is 3-4 nm for FGF-2 29) and 7-9 nm for BSA 36) . For the release of proteins based on the simple mechanism of water diffusion, smaller sized molecules appear to be easily desorbed from the polyHEMA/TMPT particles.…”

Section: Loading and Release Of Fibroblast Growth Factor-2 (Fgf-2)mentioning

confidence: 99%

Non-biodegradable polymer particles for drug delivery: A new technology for “bio-active” restorative materials

Imazato

Kitagawa

Tsuboi

et al. 2017

Dental Materials Journal

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To develop dental restorative materials with "bio-active" functions, addition of the capability to release active agents is an effective approach. However, such functionality needs to be attained without compromising the basic properties of the restorative materials. We have developed novel non-biodegradable polymer particles for drug delivery, aimed for application in dental resins. The particles are made using 2-hydroxyethyl methacrylate (HEMA) and a cross-linking monomer trimethylolpropane trimethacrylate (TMPT), with a hydrophilic nature to adsorb proteins or water-soluble antimicrobials. The polyHEMA/TMPT particles work as a reservoir to release fibroblast growth factor-2 (FGF-2) or cetylpyridinium chloride (CPC) in an effective manner. Application of the polyHEMA/ TMPT particles loaded with FGF-2 to adhesives, or those loaded with CPC to resin-based endodontic sealers or denture bases/crowns is a promising approach to increase the success of the treatments by conferring "bio-active" properties to these materials to induce tissue regeneration or to inhibit bacterial infection.

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“…Over the past two decades, topical formulations of growth factors, such as basic and acidic fibroblast growth factors (FGF) (1)(2)(3), epidermal growth factor (4,5), rhVEGF (6), insulin-like growth factor (7), and transforming growth factor-β (8), have been explored for their potential applications in wound healing. Various material, such as alginate (6), gelatin (2), fibrin (7), polyethylene glycol diacrylate (9), polylactic and glycolic acid microspheres (10), polyvinyl alcohol (11), and collagen (12), have been included in these topical formulations.…”

Section: Introductionmentioning

confidence: 99%