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Table 1 Apparent dissociation equilibrium constants (K'd) of DnaK for insulin, proinsulin and peptides

From: High affinity binding of hydrophobic and autoantigenic regions of proinsulin to the 70 kDa chaperone DnaK

Peptide/Protein (Sequence)

K'd (μM)

Human insulin (A- and B-chain)

67.8 ± 20.8

Peptide B18-30 (insulin B-chain aa18-30)

VCGERGFFYTPKT

51.9 ± 12.8

Control peptide (sigma32 aa192-204)

SHAMAPVLYLQDK

0.5 ± 0.1

Peptide B11-23 (insulin B-chain aa11-23)

LVEALYLVCGERG

2.2 ± 0.4

Human proinsulin variant

11.3 ± 7.8

  1. The DnaK affinity of insulin and insulin-derived peptides was determined in a competition assay as described in "Methods". Lines indicate the disulfide bonds in the insulin and proinsulin-molecules. The data show mean ± SD of three or four determinations.
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BMC Biochemistry

ISSN: 1471-2091

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