Regular ArticlesADAPTING PHARMACOKINETIC PROPERTIES OF A HUMANIZED ANTI-INTERLEUKIN-8 ANTIBODY FOR THERAPEUTIC APPLICATIONS USING SITE-SPECIFIC PEGYLATION
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2014, Computational and Structural Biotechnology JournalCitation Excerpt :Several branched and non-branched PEG structures have been evaluated for the effect on renal clearance. Enhanced PK profiles for branched PEG conjugates have consistently been described for therapeutic proteins in the literature [112–114]. Recently for instance, single domain antibodies labeled with 2×20 kDa PEG were shown to be superior over 1×40 kDa and 4×10 kDa labeling without affecting the biological activity [114].
Production, purificationand biological characterization of mono-PEGylated anti-IL-17A antibody fragments
2013, International Journal of PharmaceuticsCitation Excerpt :This is in part due to the fact that they have a molecular weight below the kidney filtration threshold (∼60 kDa) but also due to the lack of recycling by the neonatal Fc receptor (FcRn)-mediated recycling pathway (Roopenian and Akilesh, 2007). PEGylation of proteins is a common approach to increase serum half-life (Knight et al., 2004; Kontermann, 2009; Koumenis et al., 2000; Leong et al., 2001). The conjugation of PEG chains to proteins and antibody fragments may prolong the residence in the body due to reduced renal clearance, enhanced proteolytic resistance and reduced recognition by specific antibodies (Bailon and Won, 2009; Pasut et al., 2004; Veronese and Pasut, 2005).
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Correspondence to: Steve Leong, Maxygen, Inc., 515 Galveston Dr, Redwood City, CA 94063, USA. E-mail:[email protected]