Neonatal Fc Receptor Binding Tolerance toward the Covalent Conjugation of Payloads to Cysteine 34 of Human Albumin Variants.
Mol Pharm
; 13(2): 677-82, 2016 Feb 01.
Article
in En
| MEDLINE
| ID: mdl-26654692
ABSTRACT
The long circulatory half-life of albumin facilitated by the interaction with the cellular recycling neonatal Fc receptor (FcRn) is utilized for drug half-life extension. FcRn engagement effects following covalent attachment of cargo to cysteine 34, however, have not been investigated. Poly(ethylene glycol) polymers were used to study the influence of cargo molecular weight on human FcRn engagement of recombinant wild type (WT) albumin and an albumin variant engineered for increased FcRn binding. Decreased affinity was observed for all conjugates; however, the engineered albumin maintained an affinity above that of unmodified wild type albumin that promotes it as an attractive drug delivery platform.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Polymers
/
Recombinant Fusion Proteins
/
Serum Albumin
/
Receptors, Fc
/
Histocompatibility Antigens Class I
/
Cysteine
Limits:
Humans
Language:
En
Journal:
Mol Pharm
Journal subject:
BIOLOGIA MOLECULAR
/
FARMACIA
/
FARMACOLOGIA
Year:
2016
Document type:
Article
Affiliation country: