Functionalization of a protein surface with per-O-methylated β-cyclodextrin.

Abstract:

:Per-O-methylated β-cyclodextrin (CD) bearing an iodoacetamide group at the 6-position was synthesized to functionalize protein surfaces. Bovine serum albumin (BSA) was quantitatively modified with the CD derivative by the S(N) 2 reaction of iodoacetamide with a cysteine residue (Cys34) on the BSA surface. The resultant CD-functionalized BSA (BSA-CD) spontaneously dimerized upon addition of an anionic tetraarylporphyrin (TPPS) through the supramolecular 1:2 complexation between TPPS and CD on the protein surface. The BSA-CD/TPPS complex further complexed with ferric protoporphyrin IX (hemin) in the hydrophobic pockets of albumin to form a hemin/BSA-CD/TPPS ternary complex in which static fluorescence quenching occurred owing to intramolecular electron transfer from the photoexcited TPPS to hemin.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Kitagishi H,Kashiwa K,Kano K

doi

10.1002/bip.21695

subject

Has Abstract

pub_date

2012-01-01 00:00:00

pages

11-20

issue

1

eissn

0006-3525

issn

1097-0282

journal_volume

97

pub_type

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