Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polyclonal antibodies against glutaraldehyde-treated rabbit serum albumin (pRSA) and human serum albumin (pHSA) were prepared from rabbit and mouse, respectively. Anti-pRSA antibody had the structural determinant depending on the polymerization process of RSA and showed only a weak cross-reactivity with the other glutaraldehyde-treated albumins. Anti-pHSA antibody (after adsorption of anti-HSA antibody) recognized only pHSA, but not HSA and the other treated albumins. The cross-reactivity of those antibodies was examined with albumins treated by other methods such as modification of glucose and fructose, carbodiimide, and transglutaminase. Among the, RSA and HSA modified with glucose and fructose had an affinity for each antibody and the reactivity depended on the extent of formation of the polymerized albumin. The results suggests that functional groups involved in cross-linking of albumin are important for formation of the cross-reactivity with the antibody and that a definite structure immunochemically similar to glutaraldehyde-treated albumin could be formed by the Maillard reaction.
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PMID:Immunochemical approach to characterize post-translational modification of serum albumin using anti-glutaraldehyde-treated serum albumin antibodies. 905 74

Targeted delivery of anticancer drugs that selectively accumulate in malignant cells could enhance drug efficacy and reduce side effects of conventional chemotherapy. In this work, we designed a single domain antibody (nanobody) based drug delivery system for targeted delivery of anticancer drugs. An anti-EGFR nanobody (Nb) was constructed with a C3-tag and a Q-tag for site specific modifications under physiological conditions. The site specific PEGylation of the nanobody was achieved via a transglutaminase catalyzed reaction through the coupling of the Q-tag with PEG-NH2. As a proof of concept, the PEGylated nanobody was tethered to HSA coated upconversion nanoparticles (UCNPs) through the C3-tag, and an anticancer drug, doxorubicin (DOX), was loaded. Results showed that the Nb-conjugated drug delivery system exhibits superior specificity to the EGFR positive tumor cells. The drug delivery system is highly accumulated in the EGFR positive tumor cells (A431), whereas there was no detectable accumulation in the EGFR negative cells (MCF-7). Consequently, the drug loaded particles demonstrated significantly higher anti-proliferation to A431 cells than to MCF-7 cells. This work provides an effective approach for site-specific modification of nanobodies for the construction of targeted drug delivery systems.
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PMID:Transglutaminase mediated PEGylation of nanobodies for targeted nano-drug delivery. 3225 88