Abstract
Expression of human serum albumin in Pichia pastoris protease-deficient host and conjugation with gadolinium-diethylenetriamine pentaacetate for application as a contrast agent
Highlights
Human serum albumin (HSA) is a globular protein with a molecular weight of 66.5 kDa, which consists of 585 amino acids and 17 disulfide bonds in a single polypeptide
HSA reversibly can bind to gadolinium-diethylenetriamine pentaacetate (Gd-diethylenetriamine pentaacetate (DTPA)), resulting in significantly higher relaxivity and intravascular retention than the existing contrast agent used in magnetic resonance (Wu et al, 2007; Goyen, 2008; Zhen et al, 2012)
The HSA gene was constructed in the pD912 plasmid (DNA2.0) to form recombinant plasmid pD912-recombinant HSA (rHSA) under alcohol oxidase 1 (AOX1) promoter control with an α-factor signal sequence and subsequently cloned in E. coli TOP10F’
Summary
Human serum albumin (HSA) is a globular protein with a molecular weight of 66.5 kDa, which consists of 585 amino acids and 17 disulfide bonds in a single polypeptide. HSA is a primary protein found in blood plasma It functions as a carrier for endogenous and exogenous hydrophobic molecules such as fatty acids, bilirubin, and hormones. It acts as a flexible carrier protein for small lipophilic drug molecules (Charter and Ho, 1994; Raoufinia et al, 2016). HSA reversibly can bind to Gd-DTPA, resulting in significantly higher relaxivity and intravascular retention than the existing contrast agent used in magnetic resonance (Wu et al, 2007; Goyen, 2008; Zhen et al, 2012). One of the contrast agents containing HSA, gadofosveset, is approved for clinical use (Caravan et al, 2002)
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