Formation of disulfide bonds in proteins and peptides.

Abstract:

:For many proteins and peptides, disulfide bridges are prerequisite for their proper biological function. Many commercialized proteins are crosslinked by disulfide bridges that increase their resistance to destructive effects of extreme environment used in industrial processes or protect protein-based therapeutics from rapid proteolytic degradation. Manufacturing of these products must take into account oxidative refolding--a formation of native disulfide bonds by specific pairs of cysteines located throughout a sequence of linear protein. This review describes basic and practical aspects of oxidative folding that should be considered while designing and optimizing manufacturing of proteins using chemical synthesis, semi-synthesis and a recombinant expression.

journal_name

Biotechnol Adv

journal_title

Biotechnology advances

authors

Bulaj G

doi

10.1016/j.biotechadv.2004.09.002

subject

Has Abstract

pub_date

2005-01-01 00:00:00

pages

87-92

issue

1

eissn

0734-9750

issn

1873-1899

pii

S0734-9750(04)00088-6

journal_volume

23

pub_type

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