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Affinity of human anti‐factor VIII antibodies for functional polystyrene supports
Author(s) -
Dahri L.,
Stoltz J. F.,
BoissonVidal C.,
Muller D.,
Jozefonvicz J.
Publication year - 1996
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199634/12)9:5/6<401::aid-jmr274>3.0.co;2-n
Subject(s) - polystyrene , antibody , chemistry , immunology , medicine , organic chemistry , polymer
Abstract Human anti‐factor VIII antibodies (anti‐FVIII) neutralize Factor VIII (FVIII) procoagulant activity. These antibodies appear in about 5–15 per cent of severely affected patients with haemophilia A treated with FVIII concentrates (Mannucci, 1993). In order to obtain non‐thrombogenic materials able to interact specifically with anti‐FVIII, amino acids residues that mimic part of the FVIII molecule recognized by anti‐FVIII have been grafted. Several cross‐linked polystyrenes were functionalized with sulphonate and tyrosine sulphamide groups or tyrosine derivatives sulphamide groups such as methyl ester tyrosine, or the peptides aspartic acid methyl amide tyrosine, tyrosine aspatic acid methyl amide or aspartic acid aspatic acid methyl amide tyrosine. The in vitro removal of anti‐FVIII from haemophilic A plasma was performed on different supports. These polymers exhibit strong and selective affinity for the anti‐FVIII. The amont of adsorbed anti‐FVIII varies with the composition of the polymer and a maximum is achieved for 15–35 per cent of amino acid sulphamide groups. The influence of different chemical groups on the surface of the polymeric solid supports on the adsorption of anti‐FVIII was also studied.