Lysinonorleucine cross-link formation in alpha amino heptenoic acid-substituted peptide derivatives
✍ Scribed by Gene Karwoski; Michael Galione; Barry Starcher
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 459 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Studies on the cross‐linking of a tripeptide (t‐butyloxycarbonyl‐L‐alanyl‐D,L‐2‐amino‐6‐heptenoyl‐L‐alanine methyl ester) have shown that it is possible to form specific cross‐links in good yields through Schiff base formation of the ε amino group of lysine. The heptenoic acid residue has been ozonized to an aldehyde and condensed with the ε amino of lysine in the compounds alpha‐t‐butyloxycarbonyl‐L‐alanyl‐L‐lysine methyl ester and alpha‐t‐butyloxycarbonyl‐L‐lysine methyl ester to form the cross‐link, lysinonorleucine. This compound has been stabilized by reduction with sodium borohydride and quantitated on the amino acid analyzer. This technique converts from 60 to 98% of the available aldehyde to lysinonorleucine.