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. 2011 Apr 28;6(4):e19291. doi: 10.1371/journal.pone.0019291

Table 1. Peptides tested in this study for their crystallin aggregation properties.

Peptide Sequence Whether present in the lens Amount of human lens proteins precipitated by the peptide (µg)
αA-(1-14) CH3-MDVTIQHPWFKRTL Yes 11
αA-(67-75) DRDKFVIFL Yes 142
αA-(66-75) SDRDKFVIFL Yes 44
αA-(66-80) SDRDKFVIFLDVKHF Yes 139
αA-(66-80-Pro) SDRDKFPIFLDVKHF No 14
αA-(66-80-Ala) SDRDKFAIFLDVKHF No 103
αA-(66-80-Scr) FKISDHFKDVFRDVL No 19

Water-soluble extract (2 mg) from 35-year-old human lens was incubated in 50 mM phosphate buffer, pH 7.2 at 37°C for 24 h in the presence or absence of various peptides (25 µg). The precipitate formed was collected by centrifugation at 1000× g for 10 min and dissolved in buffer containing 7 M urea and the amount of protein was estimated by Bio-Rad protein assay method. The values are an average of two independent experiments. Lens extract alone showed the precipitation of ∼12 µg of proteins after 24 h of incubation. Bold letters in sequence represent substitutions.