Effect of oxidized βB3-crystallin peptide (152-166) on thermal aggregation of bovine lens γ-crystallins

Identification of peptide interacting sites

Padmanabha E G Udupa, Krishna K. Sharma

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Abstract

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.

Original languageEnglish
Pages (from-to)185-196
Number of pages12
JournalExperimental Eye Research
Volume80
Issue number2
DOIs
Publication statusPublished - 01-02-2005

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Crystallins
Lenses
Hot Temperature
Peptides
Propionates

All Science Journal Classification (ASJC) codes

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

Cite this

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title = "Effect of oxidized βB3-crystallin peptide (152-166) on thermal aggregation of bovine lens γ-crystallins: Identification of peptide interacting sites",
abstract = "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.",
author = "Udupa, {Padmanabha E G} and Sharma, {Krishna K.}",
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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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JO - Experimental Eye Research

JF - Experimental Eye Research

SN - 0014-4835

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