TY - JOUR
T1 - Effect of oxidized βB3-crystallin peptide (152-166) on thermal aggregation of bovine lens γ-crystallins
T2 - Identification of peptide interacting sites
AU - Udupa, Padmanabha E G
AU - Sharma, Krishna K.
PY - 2005/2/1
Y1 - 2005/2/1
N2 - We studied the effect of oxidized βB3-crystallin peptide (residues 152-166) on the thermal aggregation of bovine γ-crystallin and on chaperone activity of α-crystallin. Thermal aggregation of γ-crystallin was higher in the presence of oxidized βB3-crystallin peptide than without oxidized peptide. Increased aggregation was not observed in the presence of unoxidized βB3-crystallin peptide or a control oxidized peptide. Enhanced aggregation of γ-crystallin by oxidized βB3-crystallin peptide was observed even at 37°C. Interaction with oxidized βB3-peptide increased the hydrophobicity in the γ-crystallin as shown by increased 4, 4′-dianilino-1, 1′-binaphthyl-5, 5′-disulfonic acid (bis-ANS) binding. Enhanced aggregation of γ-crystallin was observed despite the presence of α-crystallin (a chaperone protein) in the system. Sulfo succinimidyl-2-[6-(biotinamido)-2-{p- azidobenzamido}-hexanoamido]ethyl-1-3 dithio propionate (Sulfo-SBED) cross-linker studies further confirmed the interaction between oxidized βB3-crystallin peptide and γ-crystallin. Peptide interacted sites in γ-crystallin were identified by matrix assisted laser desorption time-of-flight mass spectrometric methods and the result suggests that oxidized βB3-crystallin peptide interacted with amino acid residues present on the outer surface of the γ-crystallin. These results imply that oxidized βB3-crystallin peptide interact with γ-crystallins and enhance their aggregation and light scattering.
AB - We studied the effect of oxidized βB3-crystallin peptide (residues 152-166) on the thermal aggregation of bovine γ-crystallin and on chaperone activity of α-crystallin. Thermal aggregation of γ-crystallin was higher in the presence of oxidized βB3-crystallin peptide than without oxidized peptide. Increased aggregation was not observed in the presence of unoxidized βB3-crystallin peptide or a control oxidized peptide. Enhanced aggregation of γ-crystallin by oxidized βB3-crystallin peptide was observed even at 37°C. Interaction with oxidized βB3-peptide increased the hydrophobicity in the γ-crystallin as shown by increased 4, 4′-dianilino-1, 1′-binaphthyl-5, 5′-disulfonic acid (bis-ANS) binding. Enhanced aggregation of γ-crystallin was observed despite the presence of α-crystallin (a chaperone protein) in the system. Sulfo succinimidyl-2-[6-(biotinamido)-2-{p- azidobenzamido}-hexanoamido]ethyl-1-3 dithio propionate (Sulfo-SBED) cross-linker studies further confirmed the interaction between oxidized βB3-crystallin peptide and γ-crystallin. Peptide interacted sites in γ-crystallin were identified by matrix assisted laser desorption time-of-flight mass spectrometric methods and the result suggests that oxidized βB3-crystallin peptide interacted with amino acid residues present on the outer surface of the γ-crystallin. These results imply that oxidized βB3-crystallin peptide interact with γ-crystallins and enhance their aggregation and light scattering.
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U2 - 10.1016/j.exer.2004.08.028
DO - 10.1016/j.exer.2004.08.028
M3 - Article
C2 - 15670797
AN - SCOPUS:12744271511
SN - 0014-4835
VL - 80
SP - 185
EP - 196
JO - Experimental Eye Research
JF - Experimental Eye Research
IS - 2
ER -