Interaction of polystyrene/poly(gamma-benzyl L-glutamate) and poly(methyl methacrylate)/poly(gamma-benzyl L-glutamate) block copolymers with plasma proteins and platelets.

Abstract:

:A-B-type block copolymers, consisting of polystyrene (PST) or poly(methyl methacrylate) (PMMA) forming segment (A) and poly(gamma-benzyl L-glutamate) (P[Glu(OBzl)]) segment (B), were synthesized and the thrombus formation on these block copolymer films was investigated in relation to the adsorption of plasma proteins and the activation of platelets. The relative amount of thrombus formation was higher on homopolymers than on block copolymers. The amount of thrombus formation became less, with decreasing content of P[Glu(OBzl)] in the PST block copolymers and with increasing content of P[Glu(OBzl)] in the PMMA block copolymers. Adsorption of bovine serum albumin(BSA), bovine gamma-globulin (B gamma G) and bovine plasma fibrinogen(BPF) onto polymer films was also investigated. More proteins were adsorbed and denatured when adsorbed onto PST and PMMA than onto block copolymers. With increasing content of P[Glu(OBzl)] in the PST block copolymers, the degree of denaturation of adsorbed proteins increased, while the amount of protein adsorption was unaffected. Conversely, with increasing content of P[Glu(OBzl)] in the PMMA block copolymers, the degree of denaturation of adsorbed proteins decreased, while similarly the amount of protein adsorption was unaffected. Adhesion of platelets from platelet suspension (WP) to polymer films coated with one of the plasma proteins showed that the activation of adhered platelets was suppressed when there was a lower degree of denaturation of coated proteins. In the same experiments using platelet-rich plasma(PRP), neither the number of platelets adhered nor the degree of activation of the adhered platelets was correlated with the composition of the polymer films.(ABSTRACT TRUNCATED AT 250 WORDS)

journal_name

Biomaterials

journal_title

Biomaterials

authors

Mori A,Ito Y,Sisido M,Imanishi Y

doi

10.1016/0142-9612(86)90010-4

subject

Has Abstract

pub_date

1986-09-01 00:00:00

pages

386-92

issue

5

eissn

0142-9612

issn

1878-5905

pii

0142-9612(86)90010-4

journal_volume

7

pub_type

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