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.