Protein Formulation and Delivery by Eugene J. McNally, Eugene McNally, Jayne E. Hastedt

By Eugene J. McNally, Eugene McNally, Jayne E. Hastedt

This convenient reference presents perception into the technique used to spot the steadiness profile of a molecule that comes on the finish of the drug registration method, and provides an in-depth evaluation of the mechanisms and linked explanations of protein instability prone to be encountered in the course of drug formula development.Emphasizes the significance of choosing formula stipulations, excipients, and box closure structures to lessen degradation tactics and maximize shelf stability!Organized to direct scientists new to the sector of protein formula to acceptable beginning issues of drug improvement, Protein formula and Delivery·includes a dialogue of speeded up balance checking out and its obstacles in picking out sturdy formulations·details analytical tools universal in balance evaluation and formula development·stresses the significance of demonstrating the stability-indicating nature of an assay·describes the drug substance production method succinctly·examines preformulation and improvement of conventional resolution and lyophilized formulations meant for intravenous administration·covers aseptic processing in drug improvement and the capability improvement of a freeze-drying cycle·explores the advance of nontraditional formulations, exchange routes of drug supply, and regulated unlock dosage forms·discusses the actual and chemical features of proteins in microsphere supply systems·analyzes protein degradation mechanisms, and techniques of detecting and tracking degradation·explores formulations meant for injection, inhalation, and regulated delivery·and more!Presenting over 660 references and an intensive literature reviewvaluable to scientists at each point, Protein formula and supply is an critical advisor for business, study, and scientific pharmaceutical scientists, pharmacists, and pharmacologists; drug regulatory affairs body of workers; biotechnologists; formula, analytical, and artificial chemists and engineers; and upper-level undergraduate and graduate scholars in those disciplines.

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E. Bugg, Three-dimensional structure of recombinant human interferon. Science 252:698-702 (1991). R. G. Keck, The use of t-butyI hydToperoxide as a probe for methIOnIne oXHIation in proteins. Anal. Biochem. 236:56-62 (1996). N. P. Neumann, Oxidation with hydrogen peroxide. Methods Enzymol. 25: 393-400 (1972). W. K. Paik and S. Kim, Protein methylation: Chemical, enzymological, and biological significance. Adv. Enzymol. 42:227-286 (1975). P. K. Sysak, C. S. -Y. Ching, Chemistry of singlet oxygen.

14, 15, and 16, yields Eq. 18, which is the modified Gibbs-Helmholtz equation (for an excellent review, see Ref. 155). I1G = Mr - TI1S" + I1CiT - To - Tln(;') (18) It IS Important to remember that Eq. 18 holds true only for the two-state model, in which no stable folding intermediates exist. This assumption has been shown to be valid for many small globular proteins, although exceptions do exist (156). In some of these cases, the existence of intermediates that are not significantly populated or are short-lived cannot be ruled out.

Miskoski and N. A. Garcia, Influence of the peptide bond on the singlet molecular oxygen-mediated (02[1~g]) photooxidation of histidine and methionme dipeptIdes. A kmetIc study. Photochem. Photo bIOI. 57:447-452 (1993). M. Linetsky and B. 1. Ortwerth, Quantitation of the reactive oxygen species generated by the UVA irradiation of ascorbic acid-glycated lens proteins. Photochem. PhotobioL 63:649-655 (1996). T. Funakoshi, M. Abe, M. Sakata, S. Shoji, and Y. Kubota, The functional side of placental anticoagulant protein: Essential histidine residue of placental anticoagulant protein.

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