Figure 1. Aggregation-enhancing and
anti-chaperone property of βA3/A1102-117 peptide. A:
The effect of the βA3/A1102–117 peptide (SDAYHIERLMSFRPIC)
and the substituted peptide (SDADHGERLMSFRPIC) on thermal aggregation
of βL-crystallin shown. βL-crystallin (100 μg)
was incubated at 55 °C with 60 μg of the peptides for 60 min. βA3/A1102-117
peptide enhanced the light scattering by denaturing βL-crystallin
whereas the substituted peptide did not. A, βL-crystallin;
B, βL-crystallin + βA3/A1102–117 peptide; C, βL-crystallin
+ substituted peptide; D, βA3/A1102–117 or substituted
peptide alone. B: The effect of βA3/A1102–117
peptide (SDAYHIERLMSFRPIC) and the substituted peptide
(SDADHGERLMSFRPIC) on the chaperone-like activity of αB-crystallin
against denaturing βL-crystallin is illustrated. βL-crystallin
(100 μg) was incubated at 55 °C in the presence of 5 μg of
αB-crystallin with or without 60 μg of the peptides for 60 min. In the
presence of βA3/A1102-117 peptide, the chaperone-like
activity of αB-crystallin against denaturing βL-crystallin
was lost. The substituted peptide however, did not decrease the
chaperone-like activity of αB-crystallin. A, βL-crystallin;
B, βL-crystallin + αB-crystallin; C, βL-crystallin
+ αB-crystallin + βA3/A1102–117 peptide; D, βL-crystallin
+ αB-crystallin + substituted peptide; E, αB-crystallin + βA3/A1102–117
or substituted peptide.
Figure 1 of Rao, Mol Vis 2008; 14:666-674.