Enhancing ligand-protein binding in affinity thermoprecipitation: elucidation of spacer effects

Abstract:

:Copolymers of N-isopropylacrylamide and N-acryloyl amino acid spacers of varying chain length were synthesized. p-Aminobenzamidine (PABA) was chemically linked to the pendant carboxyl groups of these polymers to obtain thermoprecipitating affinity polymers. The inhibition constant (Ki) of these polymers for trypsin decreased, i. e., the efficiency of PABA-trypsin binding increased with increase in the spacer chain length. The polymer to which PABA was linked through a spacer of five methylene groups exhibited eleven times lower Ki than that of the polymer containing PABA without a spacer. Investigations on model inhibitors N-acyl-p-aminobenzamidines showed that this enhancement in trypsin binding by the polymers was due to the spacer as well as to microenvironmental effects. Recovery and specific activity of the trypsin recovered increased with the spacer chain length. Separation of trypsin from a mixture of trypsin and chymotrypsin was also enhanced with the spacer chain length. The inhibition constants of these affinity polymers were not adversely affected by the crowding effect. Copyright 1999 John Wiley & Sons, Inc.

journal_name

Biotechnol Bioeng

authors

Vaidya AA,Lele BS,Kulkarni MG,Mashelkar RA

doi

10.1002/(sici)1097-0290(19990820)64:4<418::aid-bit

subject

Has Abstract

pub_date

1999-08-20 00:00:00

pages

418-25

issue

4

eissn

0006-3592

issn

1097-0290

pii

10.1002/(SICI)1097-0290(19990820)64:4<418::AID-BIT

journal_volume

64

pub_type

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